SOLID ORAL PEPTIDE FORMULATIONS TECHNICAL FIELD OF THE INVENTION The present invention relates to solid compositions comprising a salt of N-(8-(2- hydroxybenzoyl)amino)caprylic acid and a further absorption enhancer, their method of preparation and their use in medicine. SEQUENCE LISTING The present application is filed with a Sequence Listing in electronic form. The entire contents of the sequence listing are hereby incorporated by reference. BACKGROUND Oral administration of peptide therapeutics has been an area of intense research and with the recent approval of Rybelsus® a first tablet product has been launched allowing patients to received GLP-1 RA treatment without the need for injection. Solid oral formulations of semaglutide have been described in various patent documents (WO2011/094531, WO2012/080471, WO2013/139694, WO2016/120378, WO2016/120380) describing the use of the absorption enhancers sodium N-(8-(2-hydroxybenzoyl)amino)caprylate or sodium caprate, whereof sodium N-(8-(2-hydroxybenzoyl)amino)caprylate is used in Rybelsus®. Most recently further improvement in tablet compositions were described in WO2019/149880 and WO/2019/21506, showing that a high ratio of SNAC optionally in combination with a hydrotrope is able to accelerate the bioavailability of semaglutide after oral dosing. Oral administration of peptides and proteins is of general interest such as in the treatment of cardiovascular disease. Two anti-PCSK9 antibodies, alirocumab/Praluent ^® and evolocumab/Repatha ^® , have been approved for the treatment of high LDL-C levels. These are administered by 1 ml subcutaneous injections every two weeks. The EGF(A) (Epidermal Growth Factor-like domain A) sequence (40 amino acids) of the LDL-R (LDL-R-(293-332)) is well recognized as the site for PCSK9 binding. The isolated wild- type EGF(A) peptide has been shown to inhibit the binding of PCSK9 to the LDL-R with an IC ₅₀ in the low µM range (Biochemical and Biophysical Research Communications 375 (2008) 69–73). This poor potency has prevented a practical pharmaceutical use of the EGF(A) peptide. Furthermore, the half-life of such peptides would be expected to be too short to be of therapeutic use. WO2012177741 and J. Mol. Biol. (2012) 422, 685-696 disclose analogues of the EGF(A) and Fc-Fusion thereof. Alternative EGF(A) peptide based PCSK9 inhibitors with an extended half-life have been disclosed in WO2017/121850. In order to increase the usability of such drugs it is of interest to develop a suitable oral formulation. Oral administration of therapeutic peptides is challenging due to the rapid degradation of such peptides in the gastrointestinal system. Solid oral formulations of PCSK9 inhibitors have recently been described in WO2021/023855 and WO2021/089761 showing that a high ratio of sodium N-(8-(2- hydroxybenzoyl)amino)caprylate (SNAC) optionally in combination with a hydrotrope is able to increase the plasma concentration of a PCSK9 inhibitor after oral dosing. Although an efficacious GLP-1 treatment has been reached, the bioavailability of the peptide therapeutic i.e. the percentage of the peptide therapeutic that reaches circulation after oral administration is still in the lower single digits compared to subcutaneous administration and thus further alternative compositions providing increased bioavailability of peptides are highly desirable. SUMMARY The present application describes that a more cost-effective product can be obtained by combing absorption enhancers. Considering the low bioavailability of a peptide therapeutic after oral administration, the amounts of API and excipients (particular absorption enhancers) are substantial, and thus the ability to reduce the amount of API and/or excipient(s) needed to reach a given level of exposure of a peptide therapeutic is advantageous. The present invention describes solid pharmaceutical compositions which includes a mix of absorption enhancers. In one embodiment the solid pharmaceutical composition comprises a salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid and a fatty acid such as a salt of capric acid. In one embodiment the solid pharmaceutical composition comprises a salt of N-(8-(2- hydroxybenzoyl)amino)caprylic acid, a fatty acid such as a salt of capric acid and a hydrotrope such as nicotinamide. In one embodiment the composition comprises a peptide therapeutic. In one embodiment the solid pharmaceutical composition comprises i) a peptide therapeutic ii) a salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), iii) a fatty acid consisting of 6-14 carbon atoms or a salt hereof and iv) nicotinamide. In one embodiment the peptide therapeutic is an acylated peptide, such as a GLP-1 receptor agonist, a PCSK9 inhibitor peptide or an insulin analogue. The peptide therapeutics may comprise one or more albumin binding moieties covalently attached to the peptides, such as in the form of a substituent comprising an albumin binding moiety. In one embodiment the solid pharmaceutical composition comprises i) a GLP-1 agonist, ii) a salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), iii) a fatty acid consisting of 6-14 carbon atoms or a salt hereof and iv) nicotinamide. In one embodiment the solid pharmaceutical composition comprises i) semaglutide or a pro-drug of semaglutide ii) a salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), iii) a fatty acid consisting of 6-14 carbon atoms or a salt hereof and iv) nicotinamide. In one embodiment the solid pharmaceutical composition comprises i) a GLP-1-GIP co-agonist, ii) a salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), iii) a fatty acid consisting of 6-14 carbon atoms or a salt hereof and iv) nicotinamide. In one embodiment the solid pharmaceutical composition comprises i) a PCSK9 inhibitor peptide, ii) a salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), iii) a fatty acid consisting of 6-14 carbon atoms or a salt hereof and iv) nicotinamide. In one embodiment the solid pharmaceutical composition comprises i) an insulin analogue, ii) a salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), iii) a fatty acid consisting of 6-14 carbon atoms or a salt hereof and iv) nicotinamide In further aspects the invention relates to medical use of a composition as described herein, such as the use in a method of treatment of diabetes, obesity and/or cardiovascular diseases. DESCRIPTION Peptide therapeutics The term “peptide” as used in the context of the invention, refers to a compound which comprises a series of amino acids interconnected by amide (or peptide) bonds. A peptide therapeutic may also herein be referred to as a therapeutic peptide and is encompassed by the term active pharmaceutical ingredient as relevant. A peptide therapeutic is a peptide-based compound suited for medical treatment, comprising at least 20 amino acid residues. In further embodiments the peptide therapeutic comprises at least 30, such as at least 40, such as at least 50 amino acid residues. In one embodiment the peptide therapeutic comprises 20-500 amino acids residues. In one embodiment the peptide therapeutic may comprise one or more modified amino acid residues and/or non- proteogenic amino acid residues. An example of a peptide therapeutics is semaglutide, and other GLP-1 agonists described below, and thus a peptide therapeutic is frequently an analogue of a naturally existing peptide. Other examples are insulin analogues and PCSK9 inhibitor peptides. In one embodiment the peptide therapeutic has an extended half-life compared to the naturally existing peptide. In one embodiment the peptide therapeutic has a plasma half-life in humans of at least 24 hours, such as at least 48 hours, such as at least 72 hours. In one embodiment the peptide therapeutic has a plasma half-life in humans of at least 96 hours, such as 120-200 hours. The plasma half-life of a peptide may be extended by attaching an albumin binding fatty acid to a peptide, which has been demonstrated for several peptide and proteins. In one embodiment the peptide therapeutic is a fatty acid substituted peptide. In one embodiment the peptide therapeutic has an albumin binding substituent. In one embodiment the peptide therapeutic comprises an albumin binding moiety. In one embodiment the peptide therapeutic comprises two albumin binding moieties. In one embodiment the peptide therapeutic is a pro-drug. In one embodiment the peptide therapeutic is a pro-drug comprising a pharmaceutical active peptide and a dipeptide moiety which is converted into a diketopiperazine moiety upon liberation of the pharmaceutical active peptide, such as those described in WO2010/071807, WO2010/080605, WO2011/163012, WO2014/152460 and WO2016/049174. In general, the term peptide therapeutic is meant to encompass compound as such and any pharmaceutically acceptable salt, amide, or ester thereof. In some embodiments the composition comprises the peptide therapeutic or a pharmaceutically acceptable salt, amide, or ester thereof. In some embodiments the composition comprises the peptide therapeutic and one or more pharmaceutically acceptable counter ions. Substituent A substituent is a moiety comprised by the peptide therapeutic. According to the invention it is preferred that the moiety e.g., the substituent has no or minimal effect on the biological functionality of the peptide therapeutic while adding other beneficial properties, such as longer half-life and/or improved exposure after oral dosing. In one embodiment the peptide therapeutic comprises a substituent comprising an albumin binding moiety. In one embodiment the peptide therapeutic comprises two substituents comprising an albumin binding moiety. In one embodiment the substituent comprising an albumin binding moiety is covalently attached to the peptide. In one embodiment the substituent comprising an albumin binding moiety is attached via a lysine residue. In one embodiment the substituent comprising an albumin binding moiety is attached to the peptide back-bone via an epsilon nitrogen of a lysine residue. In some embodiments the substituent comprises a fatty acid or a fatty diacid. In some embodiments the substituent comprises a C16, C18 or C20 fatty acid. In some embodiments the substituent comprises a C16, C18 or C20 fatty diacid. In further embodiments the albumin binding moiety is selected from the group consisting of: Chem.1: HOOC-(CH ₂ ) _n -CO-* wherein n is an integer in the range of 8-20, Chem.2: 5-tetrazolyl-(CH ₂ ) _n -CO-* wherein n is an integer in the range of 8-20, Chem.3: HOOC-(C ₆ H ₄ )-O-(CH ₂ ) _n -CO-* wherein n is an integer in the range of 6-20, Chem.4: HO-S(O) ₂ -(CH ₂ ) _n -CO-* wherein n is an integer in the range of 8-20, Chem.5: MeS(O) ₂ NH(CO)NH-(CH ₂ ) _n -CO-* wherein n is an integer in the range of 8-20 and Chem.6: 3-HO-Isoxazole-(CH ₂ ) _n -CO-* wherein n is an integer in the range of 8-20 wherein the symbol * indicates the attachment point to a linker (see further below) or the peptide. In a further embodiment the substituent comprises Chem.1: HOOC-(CH ₂ ) _n -CO-* wherein n is at least 13, such as n is 13, 14, 15, 16, 17, 18 or 19. In some embodiments n is in the range of 13 to 19, such as in the range of 13 to 17. In some embodiments n is 13, 15 or 17. In some embodiments n is 13. In some embodiments n is 15. In some embodiments n is 17. The diacid part may also be referred to using a systematic name as follows. In some embodiments the substituent comprises Chem.3: HOOC-(C ₆ H ₄ )-O-(CH ₂ ) _n -CO-* wherein n is an integer in the range of 6-14. In some embodiments the substituent comprises Chem 3b wherein the carboxy group is in position 2, 3 or 4 of the (C ₆ H ₄ ) group and wherein m is an integer in the range of 8-11. In some embodiments the substituent comprises Chem 3 or Chem 3b wherein n/m is in the range of 6 to 14, such as in the range of 8 to 11. In some embodiments the substituent comprises Chem 3 or Chem 3b, wherein n/m is 8, 10 or 12. In some embodiments the substituent comprises Chem 3 or Chem 3b, wherein n/m is 9. In some embodiments the substituent comprises Chem 3 or Chem 3b, wherein/ m is 11. Additional elements may be referred to as linkers, and it follows that the substituent may then comprise or consist of an albumin binding moiety and one or more linker elements which are referred to as linker A, linker B and linker C elements herein. The overall structure of the substituent may thus be described by the formular (I) Formular (I): Albumin binding moiety - linker A - linker B _(n=0-5 ) - linker C -* wherein linker A and linker C are optional elements, and wherein the linker B element(s) is/are individually selected and n=0-5 indicates that the substituent comprises 0, 1, 2, 3, 4 or 5 linker B elements. In one embodiment the substituent comprises a linker A element selected from Chem.7: *-NH-SO ₂ -(CH ₂ ) ₃ -CO-* or and Chem.8: -NH-CH ₂ -(C ₆ H ₁₀ )-CO- or . comprises one or more linker B elements. In one embodiment linker B element(s) is/are selected from the group consisting of: Glu, γGlu, Gly, Ser, Ala, Thr, Ado (or OEG), Aeep, Aeeep and TtdSuc. Glu, Gly, Ser, Ala, Thr are amino acid residues well known in the art. γGlu (or gGlu) is of formula Chem.9: *-NH-CH(COOH)-(CH ₂ ) ₂ -CO-* which is the same as Chem. 9b: TtdSuc is of formula Chem.10: *-NH-(CH ₂ ) ₃ -O-(CH ₂ ) ₂ -O-(CH ₂ ) ₂ O-(CH ₂ ) ₃ -NHCO* or *-NH-CH ₂ CH ₂ CH ₂ OCH ₂ CH ₂ OCH ₂ CH ₂ OCH ₂ CH ₂ CH ₂ NHCO* which is the same as Chem.10b Ado (or OEG) is of formula Chem.11: *-NH-(CH ₂ ) ₂ -O-(CH ₂ ) ₂ -O-CH ₂ -CO-* may also be referred to as 8-amino-3,6-dioxaoctanoic acid and which is the same as Chem.11b Aeep is of formula Chem.12: *NH-CH ₂ CH ₂ OCH ₂ CH ₂ OCH ₂ CH ₂ CO*, which may also be referred to as Chem.12 Aeeep is of formula Chem.13: *NH-CH ₂ CH ₂ OCH ₂ CH ₂ OCH ₂ CH ₂ OCH ₂ CH ₂ CO*, which may also be referred to as Chem.13b ε-Lys is defined by Chem.14: *-NH-(CH2)4-CH(NH2)-CO-* which may also be described by Chem.14b: In some embodiments the substituent comprises one or more 8-amino-3,6- dioxaoctanoic acid (Ado), such as two Ado elements. In some embodiments the substituent comprises one or more ε-Lys, such as two ε-Lys elements. In one embodiment the substituent may further comprise a linker C element of Chem. 15: *-NH-CH ₂ -(C ₆ H ₄ )-CH ₂ -*, which may also be referred to as ne or two substituent(s) is/are selected from the group of substituents consisting of: HOOC-(CH ₂ ) ₁₈ -CO-gGlu-2xAdo HOOC-(CH ₂ ) ₁₈ -CO-NH-CH ₂ -(C ₆ H ₁₀ )-CO-gGlu-2xAdo HOOC-(CH ₂ ) ₁₆ -CO-gGlu-2xAdo HOOC-(CH ₂ ) ₁₆ -CO-gGlu-2xAdo-NH-CH ₂ -(C ₆ H ₄ )-CH ₂ HOOC-(CH ₂ ) ₁₆ -CO-gGlu HOOC-(CH ₂ ) ₁₆ -CO-NH-CH ₂ -(C ₆ H ₁₀ )-CO-gGlu-2xAdo HOOC-(CH ₂ ) ₁₄ -CO-gGlu-2xAdo HOOC-(CH ₂ ) ₁₄ -CO-gGlu HOOC-(CH ₂ ) ₁₄ -CO-gGlu-2xAdo- HOOC-(CH ₂ ) ₁₂ -CO-gGlu-2xAdo 4-HOOC-(C ₆ H ₄ )-O-(CH ₂ ) ₁₀ -CO-gGlu-2xAdo 4-HOOC-(C ₆ H ₄ )-O-(CH ₂ ) ₁₀ -CO-gGlu-3xAdo 4-HOOC-(C ₆ H ₄ )-O-(CH ₂ ) ₁₀ -CO-gGlu 4-HOOC-(C6H4)-O-(CH2)10-CO-2xgGlu 4-HOOC-(C ₆ H ₄ )-O-(CH ₂ ) ₁₀ -CO-gGlu-3xGly 4-HOOC-(C ₆ H ₄ )-O-(CH ₂ ) ₁₀ -CO-2xgGlu-2xAdo 4-HOOC-(C ₆ H ₄ )-O-(CH ₂ ) ₁₀ -CO-gGlu-TtdSuc 4-HOOC-(C ₆ H ₄ )-O-(CH ₂ ) ₉ -CO 4-HOOC-(C ₆ H ₄ )-O-(CH ₂ ) ₁₀ -CO-gGlu-4xAdo 4-HOOC-(C ₆ H ₄ )-O-(CH ₂ ) ₁₀ -CO-NH-CH ₂ -(C ₆ H ₁₀ )-CO-gGlu-2xAdo 4-HOOC-(C ₆ H ₄ )-O-(CH ₂ ) ₉ -CO-gGlu-2xAdo 3-HOOC-(C ₆ H ₄ )-O-(CH ₂ ) ₉ -CO-gGlu-2xAdo 3-HO-Isoxazole-(CH ₂ ) ₁₂ -CO-gGlu-2xAdo HOS(O) ₂ -(CH ₂ ) ₁₅ -CO-gGlu-2xAdo-NH-CH ₂ -(C ₆ H ₄ )-CH ₂ HOS(O) ₂ -(CH ₂ ) ₁₃ -CO-gGlu-2xAdo Tetrazolyl-(CH ₂ ) ₁₅ -CO-NH-SO ₂ -(CH ₂ ) ₃ -CO-Ado-Ado-NH-CH ₂ -(C ₆ H ₄ )-CH ₂ Tetrazolyl-(CH ₂ ) ₁₂ -CO-gGlu-2xAdo Tetrazolyl-(CH ₂ ) ₁₅ -CO-gGlu-2xAdo and MeS(O) ₂ NH(CO)NH-(CH ₂ ) ₁₂ -CO-gGlu-2xAdo. HOOC-(CH ₂ ) ₁₄ -CO-gGlu-2xεLys- HOOC-(CH ₂ ) ₁₆ -CO-gGlu-2xεLys- HOOC-(CH ₂ ) ₁₈ -CO-gGlu-2xεLys- As an example, 4-HOOC-(C ₆ H ₄ )-O-(CH ₂ ) ₁₀ -CO-NH-CH ₂ -(C ₆ H ₁₀ )-CO-gGlu-2xAdo is a substituent of Formular (I) consisting of: Albumin binder moiety - linker A - linker B _(n=3) -* wherein the albumin binder moiety is Chem 3( _n=10 ), linker A is Chem.8 and the linker B elements are gGlu, and 2xAdo. In some embodiments the substituent is [2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-(17- carboxyheptadecanoylamino) butyrylamino]ethoxy}ethoxy)acetylamino] ethoxy}ethoxy)acetyl]. In some embodiments the substituent is [2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-({trans-4-[(19- carboxynonadecanoylamino)methyl]cyclohexanecarbonyl} amino)butyrylamino]ethoxy}ethoxy)acetylamino]ethoxy}ethoxy)a cetyl]. GLP-1 receptor agonists/GLP-1 agonist In one embodiment the peptide therapeutic is a GLP-1 analogue. In one embodiment the peptide therapeutic is a GLP-1 receptor agonist, also referred to as a GLP-1 agonist herein. The term “GLP-1 agonist” as used herein refers to a compound, which fully or partially activates the human GLP-1 receptor. The term is thus equal to the term “GLP-1 receptor agonist” used in other documents. The term GLP-1 agonist as well as the specific GLP-1 agonists described herein also encompass salt forms thereof. It follows that the GLP-1 agonist should display “GLP-1 activity” which refers to the ability of the compound, i.e. a GLP-1 analogue or a compound comprising a GLP-1 analogue, to bind to the GLP-1 receptor and initiate a signal transduction pathway resulting in insulinotropic action or other physiological effects as is known in the art. In some embodiments the “GLP-1 agonist” binds to a GLP-1 receptor, e.g., with an affinity constant (K _D ) or activate the receptor with a potency (EC ₅₀ ) of below 1 μM, e.g. below 100 nM as measured by methods known in the art (see e.g. WO 98/08871) and exhibits insulinotropic activity, where insulinotropic activity may be measured in vivo or in vitro assays known to those of ordinary skill in the art. For example, the GLP-1 agonist may be administered to an animal with increased blood glucose (e.g. obtained using an Intravenous Glucose Tolerance Test (IVGTT). A person skilled in the art will be able to determine a suitable glucose dosage and a suitable blood sampling regime, e.g. depending on the species of the animal, for the IVGTT) and measure the plasma insulin concentration over time. Suitable assays have been described in such as WO2015/155151. The term half maximal effective concentration (EC ₅₀ ) generally refers to the concentration which induces a response halfway between the baseline and maximum, by reference to the dose response curve. EC ₅₀ is used as a measure of the potency of a compound and represents the concentration where 50% of its maximal effect is observed. Due to the albumin binding effects of GLP-1 agonists comprising a substituent as described herein, it is important to pay attention to if the assay includes human serum albumin or not. The in vitro potency of the GLP-1 agonist may be determined as described in WO2015/155151, example 29 without Human Serum Albumin (HSA), and the EC ₅₀ determined. The lower the EC ₅₀ value, the better the potency. In one embodiment the potency (EC ₅₀ ) as determined (without HSA) is 5-1000 pM, such as 10-750 pM, 10-500 pM or 10-200 pM. In one embodiment the EC ₅₀ (without HSA) is at most 500 pM, such as at most 300 pM, such as at most 200 pM. In one embodiment the EC50 (without HSA) is comparable to human GLP-1(7-37). In one embodiment the EC ₅₀ (without HSA) is at most 50 pM. In a further such embodiment the EC ₅₀ is at most 40 pM, such as at most 30 pM such as at most 20 pM, such as at most 10 pM. In one embodiment the EC ₅₀ is around 10 pM. Also, or alternatively, the binding of the GLP-1 agonist to albumin may be measured using the in vitro potency assay of Example 29 in WO2015/155151 including HSA. An increase of the in vitro potency, EC ₅₀ value, in the presence of serum albumin reflects the affinity to serum albumin. In one embodiment the potency (EC ₅₀ ) as determined (with 1 % HSA) is 5-1000 pM, such as 100-750 pM, 200-500 pM or 100-400 pM. In one embodiment the EC ₅₀ (with 1 % HSA) is at most 750 pM, such as at most 500 pM, such as at most 400 pM, such as at most 300 or such as at most 250 pM. If desired, the fold variation in relation to a known GLP-1 receptor agonist may be calculated as EC ₅₀ (test analogue)/EC ₅₀ (known analogue), and if this ratio is such as 0.5-1.5, or 0.8-1.2 the potencies are considered to be equivalent. In one embodiment the potency, EC ₅₀ (without HSA), is equivalent to the potency of liraglutide. In one embodiment the potency, EC ₅₀ (without HSA), is equivalent to the potency of semaglutide. In one embodiment the potency, EC ₅₀ (with 1 % HSA), is equivalent to the potency of liraglutide. In one embodiment the potency, EC ₅₀ (with 1 % HSA), is equivalent to the potency of semaglutide. In some embodiments the GLP-1 agonist is a GLP-1 analogue, optionally comprising one substituent. The term "analogue" as used herein referring to a GLP-1 peptide (hereafter “peptide”) means a peptide wherein at least one amino acid residue of the peptide has been substituted with another amino acid residue and/or wherein at least one amino acid residue has been deleted from the peptide and/or wherein at least one amino acid residue has been added to the peptide and/or wherein at least one amino acid residue of the peptide has been modified. Such addition or deletion of amino acid residues may take place at the N-terminal of the peptide and/or at the C-terminal of the peptide. In some embodiments a simple nomenclature is used to describe the GLP-1 agonist, e.g., [Aib8] GLP-1(7-37) designates an analogue of GLP-1(7-37) wherein the naturally occurring Ala in position 8 has been substituted with Aib. In some embodiments the GLP-1 agonist comprises a maximum of twelve, such as a maximum of 10, 8 or 6, amino acids which have been altered, e.g., by substitution, deletion, insertion and/or modification, compared to e.g. GLP-1(7-37). In some embodiments the analogue comprises up to 10 substitutions, deletions, additions and/or insertions, such as up to 9 substitutions, deletions, additions and/or insertions, up to 8 substitutions, deletions, additions and/or insertions, up to 7 substitutions, deletions, additions and/or insertions, up to 6 substitutions, deletions, additions and/or insertions, up to 5 substitutions, deletions, additions and/or insertions, up to 4 substitutions, deletions, additions and/or insertions or up to 3 substitutions, deletions, additions and/or insertions, compared to e.g. GLP-1(7-37). Unless otherwise stated the GLP-1 agonist comprises only L-amino acids. In some embodiments the term “GLP-1 analogue” or “analogue of GLP-1” as used herein refers to a peptide, or a compound, which is a variant of the human Glucagon-Like Peptide-1 (GLP-1(7-37)). GLP-1(7-37) has the sequence HAEGTFTSDV SSYLEGQAAKEFIAWLVKGRG (SEQ ID No.: 1). In some embodiments the term “variant” refers to a compound which comprises one or more amino acid substitutions, deletions, additions and/or insertions. In one embodiment the GLP-1 agonist exhibits at least 60%, 65%, 70%, 80% or 90% sequence identity to GLP-1(7-37) over the entire length of GLP-1(7-37). As an example of a method for determination of sequence identity between two analogues the two peptides [Aib8]GLP-1(7-37) and GLP-1(7-37) are aligned. The sequence identity of [Aib8]GLP-1(7-37) relative to GLP-1(7-37) is given by the number of aligned identical residues minus the number of different residues divided by the total number of residues in GLP-1(7-37). Accordingly, in said example the sequence identity is (31-1)/31. In one embodiment the C-terminal of the GLP-1 agonist is an amide. In some embodiments the GLP-1 agonist is GLP-1(7-37) or GLP-1(7-36)amide. In some embodiments the GLP-1 agonist is exendin-4, the sequence of which is HGEGTFITSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS (SEQ ID No.: 2). In one embodiment the GLP-1 agonist is an exendin-4 analogue or an engineered peptide thereof, as disclosed in WO2013/009545 and references therein. In order to prolong the effect of the GLP-1 agonist it is preferred that the GLP-1 agonist have an extended half-life. The half-life can be determined by method known in the art an in an appropriate model, such as in Male Sprague Dawley rats or minipigs as described in WO2012/140117. Half-life in rats may be determined as in Example 39 and the half-life in minipigs may be determined as in Example 37 therein. In one embodiment the GLP-1 agonist according to the invention has a half-life above 2 hours in rat. In one embodiment the GLP-1 agonist according to the invention has a half-life above 4 hours, such as above 6 hours, such as above 8 hours, such as above 10 hours, such as above 12 hours or such as above 15 hours in rat. In one embodiment the GLP-1 agonist according to the invention has a half-life above 24 hours in minipig. In one embodiment the GLP-1 agonist according to the invention has a half- life above 30 hours, such as above 36 hours, such as above 42 hours, such as above 48 hours, such as above 54 hours or such as above 60 hours in minipig. In one embodiment the GLP-1 agonist has a molecular weight of at most 50000 Da, such as at most 40000 Da, such as at most 30000 Da. In one embodiment the GLP-1 agonist has a molecular weight of at most 20000, such as at most 10000 Da, such as at most 7500 Da, such as at most 5000 Da. In one embodiment the GLP-1 agonist has a molar mass of at most 50000 g/mol, such as at most 40000 g/mol, such as at most 30000 g/mol. In one embodiment the GLP-1 agonist has a molar mass of at most 10000 g/mol, such as at most 8000 g/mol, such as at most 6000 g/mol. In some embodiments the GLP-1 agonist comprises one substituent which is covalently attached to the peptide as described herein above. In some embodiments the substituent is [2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-(17- carboxyheptadecanoylamino) butyrylamino]ethoxy}ethoxy)acetylamino] ethoxy}ethoxy)acetyl]. In some embodiments the substituent is [2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-({trans-4-[(19- carboxynonadecanoylamino)methyl]cyclohexanecarbonyl} amino)butyrylamino]ethoxy}ethoxy)acetylamino]ethoxy}ethoxy)a cetyl]. In one embodiment the GLP-1 agonist is liraglutide. In one embodiment the GLP-1 agonist is semaglutide, also known as N-epsilon26-[2-(2- {2-[2-(2-{2-[(S)-4-carboxy-4-(17-carboxyheptadecanoylamino) butyrylamino]ethoxy}ethoxy)acetylamino]ethoxy}ethoxy)acetyl] [Aib8,Arg34]GLP-1(7-37), (SEQ ID No.: 3) which may be prepared as described in WO2006/097537, Example 4 with the following structure: In one embodiment the GLP-1 agonist is GLP-1 peptide 1 which is diacylated [Aib8,Arg34,Lys37]GLP-1(7-37) (SEQ ID No.: 4) as shown in Example 2 of WO2011/080103 and named N ^{^ ^ ^} {2-[2-(2-{2-[2-(2-{(S)-4-Carboxy-4-[10-(4- carboxyphenoxy)decanoylamino]butyrylamino}-ethoxy)ethoxy]ace tylamino}ethoxy)ethoxy]acetyl}, N ^{^ ^ ^} -{2-[2-(2-{2-[2-(2-{(S)-4-carboxy-4-[10-(4- carboxyphenoxy)decanoylamino]butyrylamino}ethoxy)ethoxy]acet ylamino}ethoxy)ethoxy]-acetyl}- [Aib ⁸ ,Arg ³⁴ ,Lys ³⁷ ]GLP-1(7-37)–peptide with the following structure. [Aib8,Glu22,Arg26,Lys27,Glu30,Arg34,Lys36]-GLP-1-(7-37)-pept idyl-Glu-Gly (SEQ ID No.: 5) as shown in Example 31 of WO2012/140117 and named N ^ε27 -[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4- [10-(4-carboxyphenoxy)decanoylamino]butanoyl]amino] ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy]-acetyl], N ^ε36 -[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-[10- (4-carboxyphenoxy)decanoylamino]- butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy]acet yl]-[Aib8,Glu22,Arg26,Lys27, Glu30,Arg34,Lys36]-GLP-1-(7-37)-peptidyl-Glu-Gly with the following structure:

In some embodiments the GLP-1 agonist is selected from one or more of the GLP-1 agonists mentioned in WO93/19175, WO96/29342, WO98/08871, WO99/43707, WO99/43706, WO99/43341, WO99/43708, WO2005/027978, WO2005/058954, WO2005/058958, WO2006/005667, WO2006/037810, WO2006/037811, WO2006/097537, WO2006/097538, WO2008/023050, WO2009/030738, WO2009/030771 and WO2009/030774. In some embodiments the GLP-1 agonist is selected from the group consisting of N- epsilon37{2-[2-(2-{2-[2-((R)-3-carboxy-3-{[1-(19-carboxynona decanoyl) piperidine-4- carbonyl]amino}propionylamino)ethoxy]ethoxy}acetylamino)etho xy]ethoxy}acetyl [desaminoHis7,Glu22,Arg26,Arg34,Lys37]GLP-1(7-37)amide; N-epsilon26{2-[2-(2-{2-[2-((R)-3- carboxy-3-{[1-(19-carboxynonadecanoyl) piperidine-4-carbonyl]amino} propionylamino)ethoxy]ethoxy}acetylamino)ethoxy] ethoxy}acetyl [desaminoHis7, Arg34] GLP-1- (7-37); N-epsilon37{2-[2-(2-{2-[2-((S)-3-carboxy-3-{[1-(19-carboxy-n onadecanoyl) piperidine-4- carbonyl]amino}propionylamino)ethoxy] ethoxy} acetylamino)ethoxy] ethoxy}acetyl[Aib8,Glu22,Arg26,Arg34,Lys37]GLP-1-(7-37)amide ; N-epsilon37-[2-(2-[2-(2-[2-(2- ((R)-3-[1-(17-carboxyheptadecanoyl)piperidin-4-ylcarbonylami no]3- carboxypropionylamino)ethoxy)ethoxy]acetylamino)ethoxy] ethoxy)acetyl][,DesaminoHis7, Glu22 Arg26, Arg 34, Phe(m-CF3)28]GLP-1-(7-37)amide; N-epsilon26-[(S)-4-carboxy-4-({trans-4-[(19- carboxynonadecanoylamino)methyl] cyclohexanecarbonyl}amino)butyryl][Aib8,Arg34]GLP-1-(7- 37); N-epsilon26-{4-[(S)-4-carboxy-4-({trans-4-[(19-carboxynonade canoylamino) methyl]cyclohexanecarbonyl} amino)butyrylamino]butyryl}[Aib8,Arg34]GLP-1-(7-37); N- epsilon26-[2-(2-{2-[(S)-4-carboxy-4-({trans-4-[(19-carboxy-n onadecanoylamino) methyl]cyclohexanecarbonyl} amino)butyrylamino]ethoxy}ethoxy)acetyl][Aib8,Arg34]GLP-1-(7 - 37); N-epsilon26-[2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-({trans-4-[(1 9-carboxy- nonadecanoylamino)methyl] cyclohexanecarbonyl}amino)butyrylamino]ethoxy}ethoxy)acetyla mino]ethoxy}ethoxy) acetyl][Aib8,Arg34]GLP-1-(7-37)amide; N-epsilon37-[2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-({trans-4- [(19-carboxy-nonadecanoylamino)methyl]cyclohexanecarbonyl}am ino) butyrylamino]ethoxy}ethoxy)acetylamino]ethoxy}ethoxy)acetyl] [Aib8,Glu22,Arg26, Arg34,Lys37]GLP-1-(7-37)amide; N-epsilon37-[2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-({trans-4-[(1 9- carboxy-nonadecanoylamino)methyl]cyclohexanecarbonyl}amino) butyrylamino] ethoxy}ethoxy)acetylamino]ethoxy}ethoxy)acetyl][DesaminoHis7 ,Glu22, Arg26,Arg34,Lys37]GLP-1-(7-37)amide; N-epsilon37-[2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-({4- [(trans-19-carboxy-nonadecanoylamino)methyl]cyclohexanecarbo nyl}amino) butyrylamino]ethoxy}ethoxy)acetylamino]ethoxy}ethoxy)acetyl] [DesaminoHis7,Arg26,Arg34,Lys3 7]GLP-1-(7-37)amide; N-epsilon37-[2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-({trans-4-[(1 9-carboxy- nonadecanoylamino)methyl]cyclohexanecarbonyl}amino) butyrylamino]ethoxy}ethoxy)acetylamino]ethoxy}ethoxy)acetyl] [DesaminoHis7,Glu22,Arg26,Arg3 4,Lys37]GLP-1-(7-37); N-epsilon26[2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-({4-[(19-carbo xy- nonadecanoylamino)methyl]cyclohexanecarbonyl}amino)butyrylam ino] ethoxy}ethoxy) acetylamino]ethoxy}ethoxy)acetyl[Aib8, Lys 26]GLP-1 (7-37)amide; N-epsilon26 [2-(2-[2-(2-[2-(2- ((S)-2-[trans-4-((9-carboxynonadecanoylamino] methyl) cyclohexylcarbonylamino]-4- carboxybutanoylamino)ethoxy)ethoxy]acetylamino) ethoxy]ethoxy)acetyl][Aib8, Lys26] GLP-1 (7- 37)amide; N-epsilon37-[2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-({trans-4-[(1 9-carboxy- nonadecanoylamino)methyl]cyclohexane-carbonyl} amino)butyrylamino]ethoxy}ethoxy)acetylamino]ethoxy}ethoxy)a cetyl] [DesaminoHis7,Arg26,Arg34,Lys37]GLP-1-(7-37); N-epsilon37-[2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4- ({trans-4-[(19-carboxy-nonadecanoylamino)methyl]cyclohexanec arbonyl} amino)butyrylamino]ethoxy}ethoxy)acetylamino]ethoxy}ethoxy)a cetyl][DesaminoHis7,Glu22,Arg2 6,Glu30,Arg34,Lys37]GLP-1-(7-37); N-epsilon26-[2-(2-{2-[(S)-4-carboxy-4-((S)-4-carboxy-4-{4-[4 - (16-(1H-tetrazol-5-yl)-hexadecanoylsulfamoyl)butyrylamino]-b utyrylamino}butyrylamino) butyrylamino] ethoxy}ethoxy)acetyl][Aib8,Arg34]GLP-1-(7-37); N-epsilon26-[2-(2-{2-[(S)-4- carboxy-4-((S)-4-carboxy-4-{12-[4-(16-(1H-tetrazol-5-yl)hexa decanoyl- sulfamoyl)butyrylamino]dodecanoylamino}butyrylamino) butyrylamino]ethoxy}ethoxy)acetyl][Aib8,Arg34]GLP-1-(7-37); N-epsilon26-[2-(2-{2-[(S)-4- carboxy-4-((S)-4-carboxy-4-{6-[4-(16-(1H-tetrazol-5-yl)hexad ecanoyl- sulfamoyl)butyrylamino]hexanoylamino} butyrylamino)butyrylamino]ethoxy}ethoxy) acetyl][Aib8,Arg34]GLP-1-(7-37); N-epsilon26-[2-(2-{2-[(S)-4-carboxy-4-((S)-4-carboxy-4-{4-[4 - (16-(1H-tetrazol-5-yl)hexadecanoylsulfamoyl)butyrylamino] butyrylamino}butyrylamino)butyrylamino]ethoxy}ethoxy)acetyl] [Aib8,Arg34]GLP-1-(7-34); N- epsilon26-[2-(2-{2-[(S)-4-carboxy-4-((S)-4-carboxy-4-{12-[4- (16-(1H-tetrazol-5- yl)hexadecanoylsulfamoyl)butyrylamino]-dodecanoylamino}butyr ylamino) butyrylamino] ethoxy}ethoxy)acetyl][Aib8,Arg34]GLP-1-(7-34); N-epsilon26-[2-(2-{2-[(S)-4-carboxy-4-((S)-4- carboxy-4-{6-[4-(16-(1H-tetrazol-5-yl)hexadecanoylsulfamoyl) butyrylamino]hexanoylamino}butyrylamino) butyrylamino]ethoxy}ethoxy)acetyl] [Aib8,Arg34]GLP- 1-(7-34); N-epsilon26-[2-(2-{2-[(S)-4-carboxy-4-((S)-4-carboxy-4-{12-[ 4-(16-(1H-tetrazol-5- yl)hexadecanoyl-sulfamoyl)butyrylamino]dodecanoylamino} butyrylamino)butyrylamino]ethoxy}ethoxy)acetyl][Aib8,Arg34]G LP-1-(7-35); N-epsilon26-[2-(2-{2- [(S)-4-carboxy-4-((S)-4-carboxy-4-{6-[4-(16-(1H-tetrazol-5- yl)hexadecanoylsulfamoyl)butyrylamino]hexanoylamino} butyrylamino)butyrylamino] ethoxy}ethoxy)acetyl][Aib8,Arg34]GLP-1-(7-35); N-epsilon26-[2-(2-{2-[(S)-4-carboxy-4-((S)-4- carboxy-4-{6-[4-(16-(1H-tetrazol-5-yl)hexadecanoylsulfamoyl) butyrylamino] hexanoylamino}butyrylamino)butyrylamino]ethoxy}ethoxy)acetyl ][Aib8,Arg34]GLP-1-(7-36)amide; N-epsilon26-[2-(2-{2-[(S)-4-carboxy-4-((S)-4-carboxy-4-{6-[4 -(16-(1H-tetrazol-5- yl)hexadecanoylsulfamoyl) butyrylamino]hexanoylamino}butyrylamino) butyrylamino]ethoxy}ethoxy)acetyl][Aib8,Arg34]GLP-1-(7-35); N-epsilon26-[2-(2-{2-[(S)-4- carboxy-4-((S)-4-carboxy-4-{12-[4-(16-(1H-tetrazol-5-yl)hexa decanoyl- sulfamoyl)butyrylamino]dodecanoylamino}butyryl-amino)butyryl amino]ethoxy} ethoxy)acetyl][Aib8,Lys33,Arg34]GLP-1-(7-34); N-epsilon26-[2-(2-{2-[(S)-4-carboxy-4-((S)-4- carboxy-4-{12-[4-(16-(1H-tetrazol-5-yl)hexadecanoylsulfamoyl )butyrylamino] dodecanoylamino}butyrylamino)butyrylamino]ethoxy}ethoxy)acet yl][Aib8,Arg34]GLP-1-(7- 36)amide; N-epsilon26-[2-(2-{2-[2-(2-{2-[2-(2-{2-[2-(2-{2-[2-(2-{2-[2- (2-{2-[(S)-4-carboxy-4-((S)-4- carboxy-4-{12-[4-(16-(1H-tetrazol-5-yl)hexadecanoylsulfamoyl ) butyrylamino]dodecanoylamino}butyrylamino) butyrylamino]ethoxy}ethoxy) acetylamino]ethoxy}ethoxy)acetylamino]ethoxy}ethoxy)acetylam ino]ethoxy}ethoxy)acetylamino]et hoxy}ethoxy)acetylamino]ethoxy}ethoxy)acetyl][Aib8,Lys26,Arg 34]GLP-1-(7-36)amide; N- epsilon37-[2-(2-{2-[(S)-4-carboxy-4-((S)-4-carboxy-4-{12-[4- (16-(1H-tetrazol-5- yl)hexadecanoylsulfamoyl)butyrylamino] dodecanoylamino}butyrylamino) butyrylamino]ethoxy}ethoxy)acetyl][Aib8,Glu22,Arg26,Arg34,Ly s37]GLP-1-(7-37)amide; N- epsilon37-[2-(2-{2-[(S)-4-carboxy-4-((S)-4-carboxy-4-{12-[4- (16-(1H-tetrazol-5- yl)hexadecanoylsulfamoyl)butyrylamino]dodecanoylamino}butyry lamino) butyrylamino] ethoxy}ethoxy)acetyl][DesaminoHis7,Glu22,Arg26,Arg34,Lys37]G LP-1-(7-37)amide; N- epsilon37{2-[2-(2-{2-[2-((R)-3-carboxy-3-{[1-(19-carboxy-non adecanoyl) piperidine-4- carbonyl]amino}propionylamino)ethoxy]ethoxy} acetylamino)ethoxy] ethoxy}acetyl [desaminoHis7,Glu22,Arg26,Arg34,Lys37]GLP-1(7-37)amide; N-epsilon37{2-[2-(2-{2-[2-((S)-3- carboxy-3-{[1-(19-carboxynonadecanoyl) piperidine-4-carbonyl]amino} propionylamino) ethoxy]ethoxy}acetylamino)ethoxy] ethoxy} acetyl [Aib8,Glu22, Arg26,Arg34, Lys37]GLP-1-(7- 37)amide; N-epsilon37-[2-(2-[2-(2-[2-(2-((R)-3-[1-(17-carboxyhepta-dec anoyl)piperidin-4- ylcarbonylamino]3-carboxy-propionylamino) ethoxy)ethoxy] acetylamino) ethoxy] ethoxy)acetyl] [DesaminoHis7, Glu22,Arg26, Arg34,Phe(m-CF3)28] GLP-1-(7-37)amide; N-epsilon37-[2-(2-{2- [2-(2-{2-[(S)-4-carboxy-4-({trans-4-[(19-carboxy-nonadecanoy lamino)methyl] cyclohexanecarbonyl} amino)butyrylamino]ethoxy} ethoxy)acetylamino] ethoxy}ethoxy)acetyl] [Aib8,Glu22,Arg26,Arg34,Lys37]GLP-1-(7-37)amide; N-epsilon37-[2-(2-{2-[2-(2-{2-[(S)-4- carboxy-4-({trans-4-[(19-carboxy-nonadecanoylamino)methyl]cy clohexane-carbonyl} amino)butyrylamino]ethoxy}ethoxy) acetylamino]ethoxy}ethoxy)acetyl] [DesaminoHis7,Glu22,Arg26,Arg34,Lys37]GLP-1-(7-37)amide; N-epsilon37-[2-(2-{2-[2-(2-{2-[(S)- 4-carboxy-4-({trans-4-[(19-carboxy-nonadecanoylamino)methyl] cyclohexanecarbonyl}amino)butyrylamino]ethoxy}ethoxy) acetylamino]ethoxy} ethoxy)acetyl] [DesaminoHis7,Glu22,Arg26,Arg34, Lys37]GLP-1-(7-37); N-epsilon37-[2-(2-{2-[2-(2-{2-[(S)-4- carboxy-4-({trans-4-[(19-carboxy-nonadecanoylamino) methyl]cyclohexane- carbonyl}amino)butyrylamino]ethoxy}ethoxy) acetylamino] ethoxy}ethoxy)acetyl] [DesaminoHis7,Glu22,Arg26,Glu30,Arg34, Lys37]GLP-1-(7-37); N-epsilon37-[2-(2-{2-[(S)-4- carboxy-4-((S)-4-carboxy-4-{12-[4-(16-(1H-tetrazol-5-yl)hexa decanoyl-sulfamoyl) butyrylamino]dodecanoylamino} butyrylamino) butyrylamino] ethoxy}ethoxy)acetyl] [Aib8,Glu22,Arg26,Arg34,Lys37]GLP-1-(7-37)amide; N-epsilon37-[2-(2-{2-[(S)-4-carboxy-4-((S)- 4-carboxy-4-{12-[4-(16-(1H-tetrazol-5-yl)hexadecanoylsulfamo yl) butyrylamino]dodecanoylamino}butyrylamino) butyrylamino] ethoxy}ethoxy)acetyl] [DesaminoHis7,Glu22,Arg26,Arg34,Lys37]GLP-1-(7-37)amide; N-epsilon37-(3-((2-(2-(2-(2-(2- Hexadecyloxyethoxy)ethoxy)ethoxy) ethoxy) ethoxy)) propionyl)[DesaminoHis7,Glu22,Arg26,Arg34,Lys37]GLP-1(7-37)- amide; N-epsilon37-{2-(2-(2-(2- [2-(2-(4-(hexadecanoylamino)-4-carboxybutyryl-amino)ethoxy) ethoxy] acetyl)ethoxy)ethoxy)acetyl)}-[desaminoHis7,Glu22,Arg26, Glu30,Arg34,Lys37] GLP-1-(7- 37)amide; N-epsilon37-{2-(2-(2-(2-[2-(2-(4-(hexadecanoylamino)-4-carbo xy-butyryl-amino) ethoxy)ethoxy]acetyl)ethoxy)ethoxy) acetyl)}-[desaminoHis7,Glu22, Arg26, Arg34,Lys37]GLP-1- (7-37)amide; N-epsilon37-(2-(2-(2-(2-(2-(2-(2-(2-(2-(octadecanoyl-amino)e thoxy)ethoxy) acetylamino)ethoxy) ethoxy)acetylamino) ethoxy)ethoxy) acetyl)[desaminoHis7,Glu22,Arg26,Arg34,Lys37] GLP-1 (7-37)amide; N-epsilon37-[4-(16-(1H- Tetrazol-5-yl)hexadecanoylsulfamoyl) butyryl] [DesaminoHis7,Glu22,Arg26, Arg34, Lys37]GLP-1- (7-37)amide; N-epsilon37-[2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-(19-carboxyno nadecanoylamino) butyrylamino] ethoxy}ethoxy) acetylamino]ethoxy} ethoxy)acetyl] [DesaminoHis7,Glu22,Arg26, Arg34,Lys37]GLP-1-(7-37); N-epsilon37-(2-{2-[2-((S)-4-carboxy-4-{(S)-4-carboxy-4-[(S)- 4- carboxy-4-(19-carboxy-nonadecanoylamino)butyrylamino]butyryl amino} butyrylamino)ethoxy]ethoxy} acetyl)[DesaminoHis7,Glu22,Arg26,Arg34,Lys37]GLP-1-(7-37); N- epsilon37-{2-[2-(2-{(S)-4-[(S)-4-(12-{4-[16-(2-tert-Butyl-2H -tetrazol-5-yl)-hexadecanoylsulfamoyl] butyrylamino}dodecanoylamino)-4-carboxybutyrylamino]-4-carbo xybutyrylamino} ethoxy)ethoxy]acetyl}[DesaminoHis7,Glu22,Arg26,Arg34,Lys37] GLP-1 (7-37); N-epsilon37-[2-(2- {2-[2-(2-{2-[(S)-4-carboxy-4-(17-carboxy-heptadecanoylamino) -butyrylamino]-ethoxy}-ethoxy)- acetylamino]-ethoxy}-ethoxy)-acetyl] [Aib8,Glu22, Arg26,Arg34,Lys37]GLP-1-(7-37); N-alpha37- [2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-(17-carboxy-heptadecanoyl amino)-butyrylamino]-ethoxy}- ethoxy)-acetylamino]-ethoxy}-ethoxy)-acetyl] [Aib8,Glu22,Arg26,Arg34,epsilon-Lys37]GLP-1-(7- 37)peptide; N-epsilon37-[2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-(17-carboxy-h eptadecanoylamino)- butyrylamino]-ethoxy}-ethoxy)-acetylamino]-ethoxy}-ethoxy)-a cetyl] [desaminoHis7, Glu22,Arg26,Arg34,Lys37] GLP-1-(7-37); N-epsilon36-[2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-(15- carboxy-pentadecanoylamino)-butyrylamino]-ethoxy}-ethoxy)-ac etylamino]-ethoxy}-ethoxy)- acetyl] [desaminoHis7, Glu22,Arg26,Glu30,Arg34,Lys36] GLP-1-(7-37)-Glu-Lys peptide; N- epsilon37-[2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-({trans-4-[(19- carboxynonadecanoylamino)methyl]cyclohexanecarbonyl}amino)bu tyryl- amino]ethoxy}ethoxy)acetylamino]ethoxy}ethoxy)acetyl][Aib8,G lu22,Arg26,Arg34,Lys37]GLP-1- (7-37); N-epsilon37-[2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-(17-carboxy-h eptadecanoylamino)- butyrylamino]-ethoxy}-ethoxy)-acetylamino]-ethoxy}-ethoxy)-a cetyl]-[Aib8,Glu22, Arg26,Arg34,Aib35,Lys37]GLP-1-(7-37); N-epsilon37-[(S)-4-carboxy-4-(2-{2-[2-(2-{2-[2-(17- carboxyheptadecanoylamino) ethoxy] ethoxy} acetylamino) ethoxy] ethoxy} acetylamino) butyryl] [Aib8,Glu22,Arg26,34,Lys37] GLP-1 (7-37); N-epsilon37-[2-(2-[2-(2-[2-(2-[4-(17- carboxyheptadecanoylamino)-4(S)-carboxybutyry- lamino]ethoxy)ethoxy]acetylamino)ethoxy]ethoxy)acetyl] [ImPr7,Glu22, Arg26,34,Lys37], GLP-1- (7-37); N-epsilon26-{2-[2-(2-{2-[2-(2-{(S)-4-carboxy-4-[10-(4-carbox yphenoxy) decanoylamino]butyrylamino}ethoxy)ethoxy] acetylamino}ethoxy) ethoxy]acetyl}, N-epsilon37-{2- [2-(2-{2-[2-(2-{(S)-4-carboxy-4-[10-(4-carboxy-phenoxy) decanoylamino] butyrylamino}ethoxy)ethoxy]acetylamino}ethoxy) ethoxy]acetyl}-[Aib8,Arg34,Lys37]GLP-1(7-37)- OH; N-epsilon26 (17-carboxyhepta-decanoyl)-[Aib8,Arg34]GLP-1-(7-37)-peptide; N-epsilon26- (19-carboxynonadecanoyl)-[Aib8,Arg34]GLP-1-(7-37); N-epsilon26-(4-{[N-(2-carboxyethyl)-N-(15- carboxypenta-decanoyl)amino]methyl}benzoyl[Arg34]GLP-1-(7-37 ); N-epsilon26-[2-(2-[2-(2-[2-(2- [4-(17-carboxyheptadecanoylamino)-4(S)-carboxybutyrylamino]e thoxy)ethoxy] acetylamino) ethoxy]ethoxy)acetyl][Aib8,Arg34]GLP-1-(7-37); N-epsilon26-[2-(2-[2-(2-[2-(2-[4-(19- carboxynonadecanoylamino)-4(S)-carboxybutyrylamino]ethoxy)et hoxy] acetylamino)ethoxy]ethoxy)acetyl][Aib8,Arg34]GLP-1-(7-37); N-epsilon26-[2-(2-[2-(2-[2-(2-[4-(17- carboxyheptadecanoylamino)-4(S)-carboxybutyrylamino]ethoxy)e thoxy] acetylamino)ethoxy]ethoxy)acetyl][3-(4-Imidazolyl)Propionyl7 ,Arg34]GLP-1-(7-37); N-epsilon26- [2-(2-[2-(2-[2-(2-[4-(17-carboxyheptadecanoylamino)-(carboxy methyl- amino)acetylamino]ethoxy)ethoxy]acetylamino)ethoxy]ethoxy)ac etyl][Aib8,Arg34]GLP-1-(7-37); N-epsilon26-[2-(2-[2-(2-[2-(2-[4-(17-carboxyheptadecanoylami no)-3(S)- Sulfopropionylamino]ethoxy)ethoxy]acetylamino)ethoxy]ethoxy) acetyl][Aib8,Arg34]GLP-1-(7-37); N-epsilon26-[2-(2-[2-(2-[2-(2-[4-(17-carboxyheptadecanoylami no)-4(S)- carboxybutyrylamino]ethoxy)ethoxy]acetylamino)ethoxy]ethoxy) acetyl][Gly8,Arg34] GLP-1-(7-37); N-epsilon26-[2-(2-[2-(2-[2-(2-[4-(17-carboxyheptadecanoylami no)-4(S)- carboxybutyrylamino]ethoxy)ethoxy]acetylamino)ethoxy]ethoxy) acetyl][Aib8,Arg34]GLP-1-(7-37)- amide; N-epsilon26-[2-(2-[2-(2-[2-(2-[4-(17-carboxyheptadecanoylami no)-4(S)- carboxybutyrylamino]ethoxy)ethoxy]acetylamino)ethoxy]ethoxy) acetyl] [Aib8,Arg34,Pro37]GLP-1- (7-37)amide; Aib8,Lys26(N-epsilon26-{2-(2-(2-(2-[2-(2-(4-(pentadecanoylam ino)-4- carboxybutyrylamino)ethoxy)ethoxy]acetyl)ethoxy) ethoxy)acetyl)}), Arg34)GLP-1 H(7-37)-OH; N- epsilon26-[2-(2-[2-(2-[2-(2-[4-{[N-(2-carboxyethyl)-N-(17- carboxyheptadecanoyl)amino]methyl}benzoyl)amino]ethoxy) ethoxy]acetylamino)ethoxy]ethoxy)acetyl][Aib8,Arg34]GLP-1(7- 37); N-alpha7-formyl, N- epsilon26-[2-(2-[2-(2-[2-(2-[4-(17-carboxyheptadecanoyl-amin o)-4(S)-carboxy- butyrylamino]ethoxy)ethoxy]acetylamino)ethoxy]ethoxy)acetyl] [Arg34]GLP-1-(7-37); N- epsilon2626-[2-(2-[2-(2-[2-(2-[4-(17-carboxyheptadecanoylami no)-4(S)-carboxy- butyrylamino]ethoxy)ethoxy]acetylamino)ethoxy]ethoxy)acetyl] [Aib8, Glu22, Arg34] GLP-1-(7-37); N-epsilon26{3-[2-(2-{2-[2-(2-{2-[2-(2-[4-(15-(N-((S)-1,3-dic arboxypropyl) carbamoyl)pentadecanoylamino)-(S)-4-carboxybutyrylamino] ethoxy)ethoxy] ethoxy}ethoxy)ethoxy]ethoxy}ethoxy)ethoxy]propionyl} [Aib8,Arg34]GLP-1-(7-37); N-epsilon26-[2- (2-[2-(2-[2-(2-[4-{[N-(2-carboxyethyl)-N-(17-carboxy- heptadecanoyl)amino]methyl}benzoyl)amino](4(S)-carboxybutyry l-amino)ethoxy) ethoxy]acetylamino)ethoxy]ethoxy)acetyl][Aib8,Arg34] GLP-1(7-37); N-epsilon26-{(S)-4-carboxy- 4-((S)-4-carboxy-4-((S)-4-carboxy-4-((S)-4-carboxy-4-(19-car boxy- nonadecanoylamino)butyrylamino)butyrylamino)butyrylamino) butyrylamino} [Aib8,Arg34]GLP-1- (7-37); N-epsilon26-4-(17-carboxyheptadecanoyl-amino)-4(S)-carboxybu tyryl-[Aib8,Arg34]GLP-1- (7-37); N-epsilon26-{3-[2-(2-{2-[2-(2-{2-[2-(2-[4-(17-carboxyheptade canoylamino)-4(S)- carboxybutyrylamino]ethoxy)ethoxy]ethoxy} ethoxy)ethoxy]ethoxy}ethoxy)ethoxy]propionyl}[Aib8,Arg34]GLP -1-(7-37); N-epsilon26-{2-(2-(2- (2-[2-(2-(4-(17-carboxyheptadecanoylamino)-4-carboxybutyryla mino) ethoxy)ethoxy]acetyl)ethoxy)ethoxy)acetyl)}-[Aib8,22,27,30,3 5,Arg34,Pro37, Lys26] GLP-1 (7- 37)amide; N-epsilon26-[2-(2-[2-[4-(21-carboxyuneicosanoylamino)-4(S)- carboxybutyrylamino]ethoxy]ethoxy)acetyl][Aib8,Arg34]GLP-1-( 7-37); and N-epsilon26-[2-(2-[2- (2-[2-(2-[4-(21-carboxyuneicosanoylamino)-4(S)-carboxybutyry lamino] ethoxy)ethoxy]acetylamino)ethoxy]ethoxy)acetyl][Aib8,Arg34]G LP-1-(7-37). The term GLP-1 agonist as used herein includes pro-drugs of GLP-1 agonists. In one embodiment the GLP-1 agonist is a pro-drug of semaglutide. In one embodiment the GLP-1 agonist is a pro-drug of semaglutide as described in WO2022/096636, such as in Example 1 therein providing: Gly-N ^α -2-[[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)bu tanoyl]amino]ethyl-Gly- semaglutide (SEQ ID No.: 26) with the structure In one embodiment the GLP-1 agonist is also a Gastric inhibitory polypeptide receptor agonist (GIP agonist). In one embodiment the GLP-1 agonist is a GLP-1/GIP receptor co-agonists as described in WO2022/018186. In one embodiment the GLP-1 agonist is selected from the group of GLP-1/GIP receptor co-agonists compounds described in WO2022/018186 In one embodiment the GLP-1 agonist is the GLP-1/GIP receptor co-agonists identical to compound 31 described in WO2022/018186 and having the amino acid sequence included as SEQ ID No.: 25 herein. In one embodiment the GLP-1 agonist is Tirzepatide. PCSK9 inhibitor peptides In one embodiment the peptide therapeutics is a PCSK9 inhibitor peptide. A PCSK9 inhibitor peptide (PCSK9i peptide) is a peptide molecule, which fully or partially prevents PCSK9 from binding to the human Low Density Lipoprotein Receptor (LDL-R). The EGF(A) LDL-R(293- 332) peptide binds PCSK9, but is not considered a PCSK9 inhibitor due to a relatively week binding to PCSK9. The EGF(A) LDL-R(293-332) peptide may also be referred to as an the EGF(A) domain of LDL-R or in short just as EGF(A) wherein the peptide is identified by the amino acid sequence: Gly-Thr-Asn-Glu-Cys-Leu-Asp-Asn-Asn-Gly-Gly-Cys-Ser-His-Val- Cys- Asn-Asp-Leu-Lys-Ile-Gly-Tyr-Glu-Cys-Leu-Cys-Pro-Asp-Gly-Phe- Gln-Leu-Val-Ala-Gln-Arg-Arg- Cys-Glu (SEQ ID No.: 6). In one embodiment the PCSK9i peptide is an EGF(A) analogue. As disclosed in WO2017/121850 certain EGF(A) analogues are potent PCSK9 inhibitor peptides, which may be measured in an ELISA assay (such as method D.1.1 page 175 of WO2017/121850) providing the apparent binding affinity of the EGF(A) analogue or a compound comprising an EGF(A) analogue reported as a K _i . A low K _i is thus characteristic for compounds with a strong inhibitory function as described in WO2017/121850. Based on the findings described in WO2017/121850 a suitable PCSK9 inhibitor has a K _i below 8 nM, such as below 5 nM. In one embodiment, the PCSK9 inhibitor has a K _i around 0.5-8 nM, or such as 0.5-5 nM or such as 1.0-4 nM when determined as described in WO2017/121850 (D.1.1). The term PCSK9 inhibitor peptide herein encompasses EGF(A) peptide analogues and derivatives hereof comprising a substituent as described herein above and may further be referred to as PCSK9 inhibitor peptide therapeutics. In some embodiment, the PCSK9 inhibitor peptide is selected from one or more of the EGF(A) peptide analogues and derivatives hereof mentioned in WO2017/121850. In one embodiment the PCSK9 inhibitor peptide comprises an amino acid sequence identified by the group of sequences defined by SEQ ID No.: 8-20. In one embodiment the PCSK9 inhibitor peptide comprises an amino acid sequence identified by the group of sequences defined by SEQ ID No.: 13-20. In one embodiment the PCSK9 inhibitor peptide comprises an amino acid sequence identified by the group of sequences defined by SEQ ID No.: 16-19. In one embodiment the PCSK9 inhibitor peptide comprises an amino acid sequence identified by the group of sequences defined by SEQ ID No.: 16. In one embodiment the PCSK9 inhibitor peptide is selected from: Compounds A to J (disclosed as Examples compounds 31, 95, 128, 133, 143, 144, 150, 151, 152 and 153 in WO2017/121850) having the structures shown below and including the SEQ ID reference for the amino acid sequence in parenthesis. In one embodiment the PCSK9 inhibitor peptide is Compound H having the following structure (SEQ ID No.: 16): Insulins In one embodiment the peptide therapeutic is an insulin. In one embodiment the peptide therapeutic is an insulin analogue. In one embodiment the insulin analogue is an acylated insulin, such as further described below. In one embodiment the acylated insulin is an insulin analogue comprising one or more substituents as described herein above. In one embodiment the insulin analogue comprises by covalent attachment, such as to a lysine residue an albumin binding substituent. Multiple examples of insulin analogues are known in the art and can be prepared as described such as in WO09115469 and WO 2016/119854. It has also previously been recognized that protease stability is beneficial in order to increase exposure after oral administration of a solid pharmaceutical composition. In one embodiment of the acylated insulin is a protease stabilised insulin. Insulin analogues are herein defined relative to the wild type sequence of the A and B chains. wherein the A chain is: Gly-Ile-VaI-GIu-GIn-Cys-Cys-Tre-Ser-Ile-Cys-Ser-Lys Tyr-Gln- Leu- Glu-Asn-Tyr-Cys-Asn or GIVEQCCTSICSLYQLENYCN (SEQ ID No.: 21) and the B chain is: Phe-Val-Asn-Gln-His -Leu-Cys-Gly-Ser-His-Leu-Val-GIu-Ala-Leu-Tyr- Leu-VaI-Cys-Gly-GIu-Arg- Gly-Phe-Phe-Tyr-Tre-Pro-Lys-Thr or FVNQHLCGSHLVEALYLVCGERGFFYTPKT (SEQ ID No.: 22). Insulin analogues comprising amino acid changes compared to the native sequences are described by indicating the chain; A or B, followed by a number specifying the position in the respective chain and finally the amino acid residue in that position is specified (by one letter code). Deletion of an amino acid residue may be described by “des”. Thus, e.g., A10C, B1C, desB30 human insulin (or alternatively A10Cys,B1Cys,desB30 human insulin or CysA10,CysB1,desThrB30 human insulin) is an analogue of human insulin where the amino acid in position 10 in the A chain is substituted with cysteine, the amino acid in position 1 in the B chain is substituted with cysteine, and the amino acid in position 30 (threonine, Thr) in the B chain is deleted. To further exemplify A14E,B25H human insulin includes two amino acid substitutions, whereby Tyr (Y) in position 14 of the A chain is substituted by Glu (E) and Pro (P) in position 25 of the B chain is substituted by His (H). In one embodiment the insulin analogue comprises a peptide sequence selected from the group consisting of: A14E, B25H, desB30 human insulin, A14E, B16H, B25H, desB30 human insulin, A14E, B25H, desB27, desB3010 human insulin and A14E, desB27, desB30 human insulin. In one embodiment of the invention, the insulin analogue comprises a side chain, generally referred to as a substituent, in the form of an acyl group on the ^-amino group of a Lys residue of the insulin amino acid sequence. In one embodiment the substituent is attached to the wild type lysine residue in position 29 of the B chain, referred to B29K. As described herein above a substituent is frequently attached to the peptide and may be described in parenthesis after the amino acid residue of attachment, such as by B29K(N ^{^} Eicosanedioyl-γGlu), which indicates that the substituent Eicosanedioyl-γGlu- is attached via the epsylon nitrogen of the lysine residue in position 29 of the B chain. In one embodiment the insulin analogue comprises 2-7, such as 1-6, 2-5 or 2-4 amino acid substitutions relative to human insulin. In one embodiment the peptide therapeutic is an insulin analogue comprising one or more substituents and 2-8 amino acid substitutions in the A and/or B chain. In one embodiment the insulin analogue comprises one or two substituents and 2-7, such as 1-6, 2-5 or 2-4 amino acid substitutions in the A and/or B chain relative to human insulin. In one embodiment the peptide therapeutic is an insulin analogue selected from the group consisting of: A14E,B25H,B29K(N ^ε Octadecanedioyl- γGlu-OEG-OEG),desB30 human insulin, A14E,B16H,B25H,B29K(N ^ε Octadecanedioyl-γGlu-OEG-OEG),desB30 human insulin, A14E,B16H,B25H,B29K(N(eps)Eicosanedioyl-γGlu-OEG-OEG),desB3 0 human insulin, A14E,B25H,desB27,B29K(N ^ε Octadecanedioyl-γGlu-OEG-OEG),desB30 human insulin, A14E,B16H,B25H,B29K(N ^ε Eicosanedioyl-γGlu),desB30 human insulin, A14E,B25H,desB27,B29K(N ^ε Octadecanedioyl-γGlu),desB30 human insulin, A14E,B25H,desB27,B29K(N ^ε Eicosanedioyl-γGlu),desB30 human insulin and A14E,B25H,desB27,B29K(N ^ε Eicosanedioyl-γGlu-OEG-OEG),desB30 human insulin, A10C,A14E,B4C,B25H,B29K(N ^ε Octadecanedioyl-γGlu-OEG-OEG),desB30 human insulin, A10C,A14E,B3C,B25H,B29K(N(eps)Octadecanedioyl-γGlu),desB30 human insulin, A10C,A14E,B4C,B25H,desB27,B29K(N ^ε Octadecanedioyl-γGlu),desB30 human insulin, A10C,A14E,B3C,B16H,B25H,B29K(N ^ε Eicosanedioyl-γGlu-OEG-OEG),desB30 human insulin, A10C,A14E,B3C,B25H,desB27,B29K(N(eps)octadecanedioyl-γGlu-O EG-OEG),desB30 human insulin, A10C,A14E,B3C,B25H,desB27, B29K(N(eps)eicosanedioyl-γGlu-OEG-OEG),desB30 human insulin, A10C,A14E,B3C,B16H,B25H,B29K(N ^ε Octadecanedioyl-γGlu-OEG-OEG),desB30 human insulin, A10C,A14E,B4C,B16H,B25H B29K(N ^ε Octadecanedioyl-γGlu-OEG-OEG),desB30 human insulin, A10C,A14E,B4C,B16H B25H,B29K(N ^ε Eicosanedioyl-γGlu-OEG-OEG),desB30 human insulin and A10C,A14E,B4C,B25H,desB27,B29K(N ^ε eicosanedioyl-γGlu-OEG-OEG),desB30 human insulin. In one embodiment the insulin analogue is insulin analogue comprises and A chain of the sequence GIVEQCCTSICSLEQLENYCN (SEQ ID NO.: 23) and/or a B-Chain of the sequence FVNQHLCGSHLVEALYLVCGERGFHYTP ( SEQ ID NO.:24 ) and the structure: As can be seen from the description above the substituent includes Chem.1 (n=16)- Chem.9-Chem.11-Chem.11 which is also specified as HOOC-(CH ₂ ) ₁₆ -CO-γGlu-Ado-Ado-in the section on substituents above. Absorption enhancers In one embodiment the composition of the invention comprises two absorption enhancers, wherein the two enhancers are a salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid and a fatty acid consisting of 6-14 carbon atoms or a salt hereof. Salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid The structural formula of N-(8-(2-hydroxybenzoyl)amino)caprylate is shown in formula (I). The absorption enhancers used in the present invention is a salt of N-(8-(2- hydroxybenzoyl)amino)caprylic acid (NAC). In some embodiments the salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid comprises one monovalent cation, two monovalent cations or one divalent cation. In one embodiment the salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid is selected from the group consisting of the sodium salt, potassium salt and/or the ammonium salt. In one embodiment the salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid is the sodium salt or the potassium salt. In one embodiment the salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid is selected from the group consisting of the sodium salt and the ammonium salt. Salts of N-(8-(2- hydroxybenzoyl)amino)caprylic acid may be prepared using the method described in e.g. WO96/030036, WO00/046182, WO01/092206, WO2008/028859. The salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid may be crystalline and/or amorphous. In some embodiments the absorption enhancer comprises the anhydrate, monohydrate, dihydrate, trihydrate, a solvate or one third of a hydrate of the salt of N-(8-(2- hydroxybenzoyl)amino)caprylic acid as well as combinations thereof. In some embodiments one absorption enhancer is the sodium salt of N-(8-(2- hydroxybenzoyl)amino)caprylic acid sodium N-(8-(2-hydroxybenzoyl)amino)caprylate (referred to as “SNAC” herein), also known as sodium 8-(salicyloylamino)octanoate. Fatty acid or salt hereof In one embodiment, the compositions according to the invention comprises a second absorption enhancer which is a medium chain fatty acid consisting of 6-14 carbon atoms or a salt hereof. In one embodiment the fatty acid consists of 8-12 carbon atoms, such as 8, 10 or 12 carbon atoms. In one embodiment the fatty acid is a saturated fatty acid. In one embodiment the absorption enhancer is capric acid or a salt hereof. Capric acid may also be referred to as decanoic acid (CH ₃ (CH ₂ ) ₈ COOH). In one embodiment the salt of capric acid is sodium caprate (i.e. CH ₃ (CH ₂ ) ₈ COONa). Composition The composition or pharmaceutical composition of the present invention is a solid or dry composition suited for administration by the oral route as described further herein below. In some embodiments the composition comprises at least one pharmaceutically acceptable excipient. The term "excipient" as used herein broadly refers to any component other than the active therapeutic ingredient(s) or active pharmaceutical ingredient(s) (API(s)) which in the present application is referred to as a peptide therapeutic. The excipient may be a pharmaceutically inert substance, an inactive substance, and/or a therapeutically or medicinally nonactive substance. The excipient may serve various purposes, e.g. as a carrier, vehicle, filler, binder, lubricant, glidant, disintegrant, flow control agent, crystallization inhibitors solubilizer, stabilizer, colouring agent, flavouring agent, surfactant, emulsifier or combinations of thereof and/or to improve administration, and/or absorption of the therapeutically active substance(s) or active pharmaceutical ingredient(s). The amount of each excipient used may vary within ranges conventional in the art. Techniques and excipients which may be used to formulate oral dosage forms are described in Handbook of Pharmaceutical Excipients, 8th edition, Sheskey et al., Eds., American Pharmaceuticals Association and the Pharmaceutical Press, publications department of the Royal Pharmaceutical Society of Great Britain (2017); and Remington: the Science and Practice of Pharmacy, 22nd edition, Remington and Allen, Eds., Pharmaceutical Press (2013). Excipients are generally selected from binders, such as polyvinyl pyrrolidone (povidone), etc.; fillers such as cellulose powder, microcrystalline cellulose, cellulose derivatives like hydroxymethylcellulose, hydroxyethylcellulose, hydroxypropylcellulose and hydroxy- propylmethylcellulose, dibasic calcium phosphate, corn starch, pregelatinized starch, etc.; lubricants and/or glidants such as stearic acid, magnesium stearate, sodium stearyl fumarate, glycerol tribehenate, etc.; flow control agents such as colloidal silica, talc, etc.; crystallization inhibitors such as Povidone, etc.; solubilizers such as Pluronic, Povidone, etc.; colouring agents, including dyes and pigments such as iron oxide red or yellow, titanium dioxide, talc, etc.; pH control agents such as citric acid, tartaric acid, fumaric acid, sodium citrate, dibasic calcium phosphate, dibasic sodium phosphate, etc.; surfactants and emulsifiers such as Pluronic, polyethylene glycols, sodium carboxymethyl cellulose, polyethoxylated and hydrogenated castor oil, etc.; and mixtures of two or more of these excipients and/or adjuvants. In some embodiments the composition comprises a binder, such as povidone; starches; celluloses and derivatives thereof, such as microcrystalline cellulose, e.g., Avicel PH from FMC (Philadelphia, PA), hydroxypropyl cellulose hydroxylethyl cellulose and hydroxylpropylmethyl cellulose METHOCEL from Dow Chemical Corp. (Midland, MI); sucrose; dextrose; corn syrup; polysaccharides; and gelatin. The binder may be selected from the group consisting of dry binders and/or wet granulation binders. Suitable dry binders are, e.g., cellulose powder and microcrystalline cellulose, such as Avicel PH 102 and Avicel PH 200. In some embodiments the composition comprises Avicel, such as Aavicel PH 102. Suitable binders for wet granulation or dry granulation are corn starch, polyvinyl pyrrolidone (povidon), vinylpyrrolidone-vinylacetate copolymer (copovidone) and cellulose derivatives like hydroxymethylcellulose, hydroxyethylcellulose, hydroxypropylcellulose and hydroxyl-propylmethylcellulose. In some embodiments the composition comprises povidone. In some embodiments the composition comprises a filler which may be selected from lactose, mannitol, erythritol, sucrose, sorbitol, calcium phosphate, such as calciumhydrogen phosphate, microcrystalline cellulose, powdered cellulose, confectioner's sugar, compressible sugar, dextrates, dextrin and dextrose. In some embodiments the composition comprises microcrystalline cellulose, such as Avicel PH 102 or Avicel PH 200. In some embodiments the composition comprises a lubricant and/or a glidant. In some embodiments the composition comprises a lubricant and/or a glidant, such as talc, magnesium stearate, calcium stearate, zinc stearate, glyceryl behenate, glyceryl debehenate, behenoyl polyoxyl-8 glycerides, polyethylene oxide polymers, sodium lauryl sulfate, magnesium lauryl sulfate, sodium oleate, sodium stearyl fumarate, stearic acid, hydrogenated vegetable oils, silicon dioxide and/or polyethylene glycol etc. In some embodiments the composition comprises magnesium stearate or glyceryl debehenate (such as the product Compritol® 888 ATO). In one embodiment the composition comprises magnesium stearate. In some embodiments the composition comprises a disintegrant, such as sodium starch glycolate, polacrilin potassium, sodium starch glycolate, crospovidon, croscarmellose, sodium carboxymethylcellulose or dried corn starch. The composition may comprise one or more surfactants, for example a surfactant, at least one surfactant, or two different surfactants. The term “surfactant” refers to any molecules or ions that are comprised of a water-soluble (hydrophilic) part, and a fat-soluble (lipophilic) part. The surfactant may e.g. be selected from the group consisting of anionic surfactants, cationic surfactants, nonionic surfactants, and/or zwitterionic surfactants. In some embodiment the composition comprises a hydrotrope, such as Resorcinol, Pyrocatechol, Pyrogallol, Gentisic acid, Xylenesulfonate, p-toluenesulfonate, Nicotinamide, Dimethylbenzamide, Diethylbenzamide, 1-methylnicotinamide, Salicyclic acid and P- Hydroxybenzoic acid. In one embodiment the hydrotrope is nicotinamide and/or Resorcinol. In a further embodiment the hydrotrope is nicotinamide. In a further embodiment the hydrotrope is not sodium benzoate. Dosage form The composition may be administered in several dosage forms, for example as a tablet, a coated tablet, a sachet or a capsule, such as hard or soft shell gelatine capsules, and all such compositions are considered solid oral dosage forms. A dose unit refers to a single entity to be administered such as a tablet, and the amounts of each ingredient comprised by a dose unit thus refers to the content of a single entity, such as one tablet. The composition may be in the form of a dose unit, such as a tablet. In some embodiments, the weight of the unit dose is in the range of 50 to 2000 mg, such as 50 mg to 1200 mg, such as in the range of 50-1000 mg, or such as in the range of 100-800 mg. In some embodiments the weight of the unit dose is in the range of 50 mg to 1000 mg, such as in the range of 50-750 mg, or such as in the range of 100-600 mg. In some embodiments the weight of the dose unit is in the range of 75 mg to 400 mg. In an embodiment the weight of the unit dose is in the range of 100-400 mg, such as in the range of 100-300 mg or such as in the range of 150-350 mg. In an embodiment the weight of the dose unit is in the range of 300 mg to 800 mg, such as in the range of 400-700 mg or such as in the range of 500-600 mg. In some embodiment, the weight of the unit dose is 300 to 600 mg, such as approximately 350 mg, 450 mg or 550 mg. The pharmaceutical composition according to the invention is preferably produced in a dosage form suitable for oral administration as described herein below. In the following the absolute amounts of the ingredients of the composition of the invention are provided with reference to the content in a dosage unit i.e. per tablet, capsule or sachet. The pharmaceutical compositions of the invention in an embodiment comprises 0.1-100 mg of the peptide therapeutic per dose unit. In one embodiment a dose unit of the composition comprises an amount of the peptide therapeutic is in the range of 1 – 100 mg, 20 to 100 mg, 40 to 100 mg or 50 to 85 mg. In one embodiment a dose unit of the composition comprises an amount of the peptide therapeutic is in the range of 0.1 – 50 mg, 0.2 to 50 mg, 0.5 to 50 mg or 1 to 40 mg. In one embodiment a dose unit of the composition comprises an amount of the peptide therapeutic is in the range of 0.1 – 50 mg, 0.1 – 40 mg, 0.1 – 30 mg or 0.1 – 20 mg. The pharmaceutical compositions of the invention in an embodiment comprise comprises 0.1-100 mg of the GLP-1 agonist per dose unit. In one embodiment a dose unit of the composition comprises an amount of GLP-1 agonist is in the range of 0.1 – 50 mg, 0.2 to 50 mg, 0.5 to 50 mg or 1 to 40 mg. In one embodiment a dose unit of the composition comprises an amount of GLP-1 agonist is in the range of 0.1 – 50 mg, 0.1 – 40 mg, 0.1 – 30 mg or 0.1 – 20 mg. In one embodiment a dose unit comprises 0.5-5 mg of the GLP-1 agonist, such as 0.75- 4 ½ mg, such as 1, 1 ½, 2, 2 ½ or 3 mg or 3 ½, 4, 4 ½ mg, such as 1-3 or 3-5 mg of the GLP-1 agonist per dose unit. In one embodiment a dose unit comprises 2 to 20 mg of the GLP-1 agonist, such as 2- 15 mg, such as 2, 3, 4 or 5 mg, or such as 8, 10, 12 or 14 mg, such as 15 mg or such as 20 mg of the GLP-1 agonist per dose unit. In one embodiment a dose unit comprises 25 to 100 mg of the GLP-1 agonist, such as 10-90 mg, or such as 20-60 such as 20, 30 or 40 mg, or such as 40-80 mg of the GLP-1 agonist, such as 60, 70, or 80 mg, per dose unit. In one embodiment a dose unit comprises 10 to 75 mg of the GLP-1 agonist, such as 10-70 mg, such as 20, 30 or 40 mg, or such as 50, 60, or 65 mg, or such as 20-60 mg or such as 30-50 mg of the GLP-1 agonist per dose unit. In one embodiment a dose unit comprises 5 to 50 mg of the GLP-1 agonist, such as 10- 45 mg, such as 20, 30 or 40 mg, or such as 25, 35, or 45 mg, or such as 30-50 mg or such as 20-40 mg of the GLP-1 agonist per dose unit. In an embodiment, a dose unit of the pharmaceutical compositions of the invention comprises 0.1-200 mg, 0.1-150 mg or 0.2-100 mg of the PCSK9 inhibitor. In some embodiments, a dose unit of the composition comprises an amount of PCSK9 inhibitor is in the range of 0.5-150 mg, 0.5-120 mg, 0.5-100 mg, 1-80 mg, 1-70 mg, 1-60, 1-50 mg or 1-40 mg. In some embodiments, a dose unit of the composition comprises an amount of PCSK9 inhibitor is in the range of 0.1-50 mg, 0.2-50 mg, 1-50 mg or 10-50 mg. In some embodiments, a dose unit of the composition comprises an amount of PCSK9 inhibitor is in the range of 0.1-50 mg, 0.1-40 mg, 0.1-30 mg or 0.1-20 mg. In some embodiments, a dose unit comprises 1-80 mg of the PCSK9 inhibitor, such as 2-70 mg, such as 10, 15, 20, 25 or 30 mg or 35, 40, 45 mg, such as 10-30 or 30-50 mg of the PCSK9 inhibitor per dose unit. In some embodiments, a dose unit comprises 20-200 mg of the PCSK9 inhibitor, such as 20-150, such as 20-120 mg, such as 20-100 mg, such as 20-80 mg, or such as 20, 30, 40, 50, 60, 70 or 80 mg, or such as 90, 95, 100, 105 or 110 mg, or such as 30-100 mg or such as 40-80 mg of the PCSK9 inhibitor per dose unit. In some embodiments, a dose unit comprises 10-80 mg of the PCSK9 inhibitor, such as 10-70 mg, such as 20, 30 or 40 mg, or such as 50, 60, 70 or 80 mg, or such as 30-60 mg or such as 20-50 mg of the PCSK9 inhibitor per dose unit. The amount of PCSK9 inhibitor may be varied depending on identity of the PCSK9 inhibitor and the effect desired. The pharmaceutical compositions of the invention in an embodiment comprise at most 1000 mg of said salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as sodium N- (8-(2-hydroxybenzoyl)amino)caprylate (SNAC) per dose unit. In one embodiment the composition comprises at most 800, such as at most 600 mg of said salt. In one embodiment the amount of salt of NAC is at least 20 mg or 25 mg, such as at least 50 mg, at least 75 mg, at least 100 mg, at least 125 mg, at least 150 mg, at least 175 mg, at least 200 mg, at least 225 mg, at least 250 mg, at least 275 mg and at least 300 mg per dose unit. In one embodiment the amount of salt of NAC, is up to 800 mg, such as up to 750 mg, up to 700, up to 650 mg, up to 600 mg, up to 550 mg, up to 500 mg, up to 450 mg, up to 400 mg, up to 350 mg, or such as up to 300 mg per dose unit. In one embodiment the amount of salt of NAC, is in the range of 30-500 mg, such as from 40-400 mg, such as from around 50 to around 300 mg per dose unit. In one embodiment, the amount of salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC) per dose unit of the composition is up to 3.3 mmol. In some embodiments, the composition comprises up to 2.66 mmol, such as up to 1.99 mmol of said salt. In one embodiment, the salt of NAC is at least 0.07 or 0.08 mmol, such as at least 0.17 mmol, at least 0.25 mmol, at least 0.33 mmol, at least 0.41 mmol, at least 0.50 mmol, at least 0.58 mmol, at least 0.66 mmol, at least 0.75 mmol, at least 0.83 mmol, at least 0.91 mmol, at least 1.0 mmol per unit dose. In one embodiment, the amount of salt of NAC is up to 2.66 mmol, such as up to 2.49 mmol, up to 2.32 mmol, up to 2.16 mmol, up to 1.99 mmol, up to 1.83 mmol, up to 1.66 mmol, such as up to 1.49 mmol, up to 1.33 mmol, up to 1.16 mmol or such as up to 1.00 mmol per dose unit. In one embodiment, the amount of salt of NAC is in the range of 0.10-1.66 mmol, such as 0.13-1.33 mmol, such as from around 0.17 mmol to around 1.00 mmol per dose unit. In some embodiments, the salt of NAC is SNAC. In some embodiments, the amount of SNAC in the composition is at least 20 mg, such as at least 25 mg, such as at least 50 mg, such as at least 75 mg, at least 100 mg, at least 125 mg, at least 150 mg, at least 175 mg, at least 200 mg, at least 225 mg, at least 250 mg, at least 275 mg and at least 300 mg per dose unit. In some embodiments, the amount of SNAC in the composition is up to 1000 mg, such as up to 800 mg, such as up to 600 mg, such as up to 575 mg, such as up to 550 mg, up to 525 mg, up to 500 mg, up to 475 mg, up to 450 mg, up to 425 mg, up to 400 mg, up to 375 mg, up to 350 mg, up to 325 mg per dose unit, or up to 300 mg per dose unit. In some embodiments, the amount of SNAC in the composition is in the range of 20-800 mg, such as 25-600 mg, such as 50-500 mg, such as 50-400 mg, such as 75-400 mg, such as from 80-350 mg, such as from around 100 to around 300 mg per dose unit. In one embodiment, where the salt of NAC is SNAC, the amount of SNAC is in the range of 20-200 mg, such as 25-175 mg, such as 75-150 mg, such as 80-120 mg such as around 100 mg per dose unit. In one embodiment, where the salt of NAC is SNAC, the amount of SNAC is in the range of 50-400 mg, such as 75-300 mg, such as 100-300 mg, such as 150-250 mg, such as around 200 mg per dose unit. In one embodiment, where the salt of NAC is SNAC, the amount of SNAC is in the range of 200-800 mg, such as 250-400 mg, such as 250-350 mg, such as 275-325 mg, such as around 300 mg per dose unit. For optimal effect the amount of the second absorption enhance is to be balanced, with the amount of the salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid but in general the formulation according to the invention comprise at most 1000 mg of the second absorption enhancer, such as the fatty acid or a salt thereof, such as sodium caprate. In one embodiment the composition comprises at most 800 mg, such as at most 600 mg of said second enhancer. In one embodiment the composition comprises at most 1000 mg, such as at most 800 mg, such as at most 600 mg of the fatty acid or a salt hereof, such as sodium caprate. In one embodiment the amount of the second enhancer, the fatty acid or a salt thereof is at least 20 or at least 25 mg, such as at least 50 mg, at least 75 mg, at least 100 mg, at least 125 mg, at least 150 mg, at least 175 mg, at least 200 mg, at least 225 mg, at least 250 mg, at least 275 mg and at least 300 mg per dose unit. In one embodiment the amount of the second enhancer, the fatty acid or a salt thereof, is up to 800 mg, such as up to 750 mg, up to 700 mg, up to 650 mg, up to 600 mg, up to 550 mg, up to 500 mg, up to 450 mg, up to 400 mg, up to 350 mg, or up to 300 mg per dose unit. In one embodiment the amount of the second enhancer, the fatty acid or a salt thereof is in the range of 30-500 mg, such as from 40-400 mg, such as from around 80 to around 300 mg per dose unit. The pharmaceutical compositions of the invention in an embodiment comprise at most 5.1 mmol of the second absorption enhancer, such as the medium chain fatty acid or a salt thereof, such as sodium caprate. In one embodiment, the composition comprises at most 4.12 mmol, such as at most 3.09 mmol of said second enhancer. In one embodiment, the composition comprises at most 5.1 mmol, such as at most 4.12 mmol, such as at most 3.09 mmol of the medium chain fatty acid or a salt hereof, such as sodium caprate. In one embodiment, the amount of the second enhancer, the medium chain fatty acid or a salt thereof, such as sodium caprate, is at least 0.10 or 0.13 mmol, such as at least 0.26 mmol, at least 0.39 mmol, at least 0.51 mmol, at least 0.64 mmol, at least 0.77 mmol, at least 0.90 mmol, at least 1.03 mmol, at least 1.16 mmol, at least 1.29 mmol, at least 1.42 mmol and at least 1.54 mmol per dose unit. In one embodiment, the amount of the second enhancer, the medium chain fatty acid or a salt thereof, such as sodium caprate is up to 4.12 mmol, such as up to 3.86 mmol, up to 3.60 mmol, up to 3.35 mmol, up to 3.09 mmol, up to 2.83 mmol, up to 2.57 mmol, up to 2.32 mmol, up to 2.06 mmol, up to 1.80 mmol, or up to 1.54 mmol per dose unit. In one embodiment, the amount of the second enhancer, the medium chain fatty acid or a salt thereof, such as sodium caprate is in the range of 0.15-2.57 mmol, such as from 0.21-2.06 mmol, such as from around 0.41 to around 1.54 mmol per dose unit. In some embodiments, the second enhancer is a salt of capric acid, such as sodium caprate. In some embodiments, the amount of sodium caprate in the composition is at least 20 mg or 25 mg, such as at least 50 mg, such as at least 75 mg, at least 100 mg, at least 125 mg, at least 150 mg, at least 175 mg, at least 200 mg, at least 225 mg, at least 250 mg, at least 275 mg and at least 300 mg per dose unit. In some embodiments, the amount of sodium caprate in the composition is up to 1000 mg, such as up to 800 mg, such as up to 600 mg, such as up to 575 mg, such as up to 550 mg, up to 525 mg, up to 500 mg, up to 475 mg, up to 450 mg, up to 425 mg, up to 400 mg, up to 375 mg, up to 350 mg, up to 325 mg per dose unit, or up to 300 mg per dose unit. In some embodiments, the amount of sodium caprate in the composition is in the range of 20-800 mg, such as 25-600 mg, such as 50-500 mg, such as 50-400 mg, such as 75-400 mg, such as from 80-350 mg, such as from around 100 to around 300 mg per dose unit. In one embodiment, where the salt of capric acid is sodium caprate, the amount of sodium caprate is in the range of 20-200 mg, such as 30-175 mg, such as 75-150 mg, such as 80-120 mg such as around 100 mg per dose unit. In one embodiment, where the salt of capric acid is sodium caprate, the amount of sodium caprate is in the range of 50-400 mg, such as 75-300 mg, such as 100-300 mg, such as 150-250 mg, such as around 200 mg per dose unit. In one embodiment, where the salt of capric acid is sodium caprate, the amount of sodium caprate is in the range of 200-800 mg, such as 250-400 mg, such as 250-350 mg, such as 275-325 mg, such as around 300 mg per dose unit. In one embodiment the amounts (w) of the two absorption enhancers differs with at most a factor 10, such as a factor 5, such as a factor 2. In one embodiment the ratio of SNAC/sodium caprate (w/w) is at least 0.1. In one embodiment the weight ratio (w/w), i.e. the ratio of the amount (w) of a salt of NAC to the amount (w) of a salt of the fatty acid is 0.1-10, such as 0.2-8, such as 0.3-5, such as 0.3-3, such as 0.4-2.5 or such as 0.5-2. In one embodiment the weight ratio (w/w) of SNAC to sodium caprate is 0.1-10, such as 0.2-8, such as 0.3-5. In one embodiment the weight ratio (w/w) of SNAC to sodium caprate is 0.3-3, such as 0.4-2.5 or such as 0.5-2. In one embodiment the weight ratio (w/w) of SNAC to sodium caprate is 0.6-1.9, or such as 0.5-1.8, or such as 0.8-1.7. In one embodiment the weight ratio (w/w) of SNAC to sodium caprate is 0.8-1.6, or such as 0.8-1.5, or such as 0.8-1.4. In one embodiment the weight ratio (w/w) of SNAC to sodium caprate is 0.9-1.3, or such as 0.9-1.2, or such as 0.8-1.3, or such as 0.8-1.2. For optimal effect the amount of the second absorption enhancer is to be approximately 1:1 with the amount (w) of the salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid. The amount of the hydrotrope is to be balanced with the amount of the absorption enhancers, such as one or more of the salt of NAC and/or the salt of capric acid, but in general a dose unit of the compositions of the invention comprises 10-600 mg of the hydrotrope. In on embodiment the composition comprises 10-400 mg of the hydrotrope. In one embodiment, a dose unit comprises 20-400 mg, such as 40-300, such as 50-200 mg, such as 50-175 mg of the hydrotrope. In some embodiment, a unit dose comprises 10-600 mg, such as 15-500 mg or such as 20-400 mg of the hydrotrope. In some embodiment, a unit dose comprises 70-155 mg, such as 70-105 mg or 70-100 mg of the hydrotrope. In some embodiment, a unit dose comprises 70-105 mg or 100-155 mg of the hydrotrope. In one embodiment, a dose unit comprises 100-600 mg, such as 100-500, such as 150-400 mg, such as 150-300 mg of the hydrotrope. In one embodiment a dose unit comprises 10-200 mg, such as 15-175, such as 20-150 mg, such as 20-125 mg of the hydrotrope. In some embodiment, a unit dose comprises 20-200 mg, 30-200 mg, 40-200 mg, 50- 200 or such as 75-200 mg of the hydrotrope. In some embodiment, a unit dose comprises 20-175 mg or 30-150 mg of the hydrotrope. In further such embodiments, a unit dose of the composition according to the invention comprises 50-600 mg nicotinamide and/or resorcinol. In one embodiment, a dose unit comprises 10-200 mg, such as 15-175, such as 20-150 mg, such as 25-150 mg nicotinamide and/or resorcinol. In one embodiment, a dose unit comprises 50-400 mg, such as 50-300, such as 50-200 mg, such as 50-175 mg nicotinamide and/or resorcinol. In further such embodiments, a unit dose of the composition comprises 50-600 mg nicotinamide. In one embodiment, a dose unit comprises 50-400 mg, such as 50-300, such as 50-200 mg, such as 50-175 mg nicotinamide. In one embodiment, a unit dose comprises 70-155 mg, such as 70-105 mg or 70-100 mg nicotinamide. In some embodiment, a unit dose comprises 70-155 mg, such as 100-155 mg nicotinamide In further such embodiments, a unit dose of the composition according to the invention comprises 10-400 mg nicotinamide and/or resorcinol. In one embodiment a dose unit comprises 10-200 mg, such as 20-175, such as 20-150 mg, such as 20-125 mg nicotinamide and/or resorcinol. In some embodiment, a unit dose comprises 20-200 mg, 30-200 mg, 40-200 mg, 50- 200 or such as 75-200 mg nicotinamide and/or resorcinol. In some embodiment, a unit dose comprises 20-175 mg or 30-150 mg nicotinamide and/or resorcinol. In further such embodiments a unit dose of the composition comprises 10-400 mg nicotinamide. In one embodiment a dose unit comprises 10-200 mg, such as 20-175, such as 20- 150 mg, such as 20-125 mg nicotinamide. In some embodiment, a unit dose comprises 20-200 mg, 30-200 mg, 40-200 mg, 50- 200 or such as 75-200 mg nicotinamide. In some embodiment, a unit dose comprises 20-175 mg or 30-150 mg nicotinamide. In one embodiment, the weight ratio of the amount (w) of salt of NAC to the amount (w) of the hydrotrope is at least 0.5. In one embodiment the weight ratio of the amount (w) of salt of NAC to the amount (w) of the hydrotrope is 0.5-10, such as 0.5-5 or such as 1-5. In one embodiment the weight ratio of the amount (w) of salt of NAC to nicotinamide (w) is 0.5-10, such as 0.5-5 or such as 1-5. In one embodiment, the weight ratio of the amount (w) of salt of NAC to nicotinamide (w) is 0.5-10, such as 0.5-5 or such as 1-5. In one embodiment the ratio of the amount (w) of salt of NAC to the amount (w) of nicotinamide is 1-2, such as 1.2-1.8 or such as 1.3-1.7 or such as 1.4-1.6. In one embodiment, a unit dose of the composition further comprises 0.5-50 mg of a lubricant, such as 0.10-25 mg, such as 0.25-10 mg, such as 0.5-8 mg lubricant. In one embodiment, a unit dose of the composition comprises 0.5-50 mg of magnesium stearate, such as 0.10-25 mg, such as 0.25-10 mg, such as 0.5-8 mg or such as 0.5-5 mg magnesium stearate. In one embodiment, a unit dose of the composition comprises 1-10 mg magnesium stearate, such as 2-8 mg or 3-7 mg. In a preferred embodiment, a unit dose of the composition comprises 20-600 mg SNAC, 20-600 mg sodium caprate, 0.5-100 mg GLP-1 agonist, 10-600 mg hydrotrope and 0.10-50 mg lubricant. In a preferred embodiment, a unit dose of the composition comprises 20-600 mg SNAC, 20-600 mg sodium caprate, 1.0-90 mg GLP-1 agonist, 10-500 mg hydrotrope and 0.10-40 mg lubricant. In a preferred embodiment, a unit dose of the composition comprises 40-600 mg SNAC, 40-600 mg sodium caprate, 5-80 mg GLP-1 agonist, 30-400 mg hydrotrope and 0.10-40 mg lubricant. In a preferred embodiment, a unit dose of the composition comprises 50-300 mg SNAC, 50-300 mg sodium caprate, 10-80 mg GLP-1 agonist, 40-300 mg hydrotrope and 2-8 mg lubricant. In a preferred embodiment, a unit dose of the composition comprises 20-600 mg SNAC, 20-600 mg sodium caprate, 10-80 mg GLP-1 agonist, 10-500 mg nicotinamide and 0.10-50 mg magnesium stearate. In a preferred embodiment, a unit dose of the composition comprises 30-500 mg SNAC, 30-500 mg sodium caprate, 10-50 mg GLP-1 agonist, 20-400 mg nicotinamide and 0.10-25 mg magnesium stearate. In a preferred embodiment, a unit dose of the composition comprises 50-300 mg SNAC, 50-300 mg sodium caprate, 10-80 mg GLP-1 agonist, 40-250 mg nicotinamide and 2-8 mg magnesium stearate. In a preferred embodiment, a unit dose of the composition comprises 90-250 mg SNAC, 90-250 mg sodium caprate, 10-80 mg GLP-1 agonist, 50-170 mg nicotinamide and 3-7 mg magnesium stearate. In a preferred embodiment, a unit dose of the composition comprises 20-600 mg SNAC, 20-600 mg sodium caprate, 0.50-50 mg GLP-1 agonist, 15-500 mg hydrotrope and 0.10-40 mg lubricant. In a preferred embodiment, a unit dose of the composition comprises 20-600 mg SNAC, 20-600 mg sodium caprate, 0.50-25 mg GLP-1 agonist, 15-500 mg hydrotrope and 0.10-40 mg lubricant. In a preferred embodiment, a unit dose of the composition comprises 25-600 mg SNAC, 25-600 mg sodium caprate, 1-75 mg GLP-1 agonist, 20-500 mg hydrotrope and 0.10-40 mg lubricant. In one embodiment the composition comprises: i) 0.5-100 mg GLP-1 agonist, ii) 20-1000 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 20-1000 mg a fatty acid consisting of 6-14 carbon atoms, such capric acid, or a salt hereof such as sodium caprate iv) 10-750 mg, such as 50-200 mg, nicotinamide or resorcinol and v) 0-25 mg lubricant. In one embodiment the composition comprises: vi) 0.5-100 mg GLP-1 agonist, vii) 25-1000 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), viii) 25-1000 mg a fatty acid consisting of 6-14 carbon atoms, such capric acid, or a salt hereof such as sodium caprate ix) 15-750 mg, such as 50-200 mg, nicotinamide or resorcinol and x) 0-25 mg lubricant. In one embodiment the composition comprises: i) 1-75 mg GLP-1 agonist, ii) 25-300 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 25-300 mg a fatty acid consisting of 6-14 carbon atoms,, such capric acid, or a salt hereof such as sodium caprate iv) 15-200 mg nicotinamide and v) 0-10 mg lubricant. In one embodiment the composition comprises: i) 1-75 mg GLP-1 agonist, ii) 25-200 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 25-200 mg sodium caprate iv) 15-150 mg nicotinamide and v) 0-10 mg magnesium stearate. In one embodiment the composition comprises: i) 1-50 mg GLP-1 agonist, ii) 25-100 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 25-100 mg sodium caprate, iv) 15-75 mg nicotinamide and v) 0-10 mg magnesium stearate. In one embodiment the composition comprises: i) 1-10 mg GLP-1 agonist, ii) 20-40 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 20-40 mg sodium caprate iv) 15-30 mg nicotinamide and v) 0-5 mg magnesium stearate. In one embodiment the composition comprises: i) 1-20 mg GLP-1 agonist, ii) 50-75 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 50-75 mg sodium caprate iv) 30-50 mg nicotinamide and v) 0-3 mg magnesium stearate. In one embodiment the composition comprises: i) 10-50 mg GLP-1 agonist, ii) 100-150 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 100-150 mg sodium caprate, iv) 70-100 mg nicotinamide and v) 0-10 mg magnesium stearate. In one embodiment the composition comprises: i) 10-80 mg GLP-1 agonist, ii) 150-250 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 150-250 mg sodium caprate, iv) 100-180 mg nicotinamide and v) 0-10 mg magnesium stearate. In a preferred embodiment, a unit dose of the composition comprises 20-600 mg SNAC, 20-600 mg sodium caprate, 0.5-100 mg PCSK9 inhibitor, 10-600 mg hydrotrope and 0.10-50 mg lubricant. In a preferred embodiment, a unit dose of the composition comprises 20-600 mg SNAC, 20-600 mg sodium caprate, 1.0-90 mg PCSK9 inhibitor, 20-500 mg hydrotrope and 0.10-40 mg lubricant. In a preferred embodiment, a unit dose of the composition comprises 40-600 mg SNAC, 40-600 mg sodium caprate, 5-80 mg PCSK9 inhibitor, 30-400 mg hydrotrope and 0.10-40 mg lubricant. In a preferred embodiment, a unit dose of the composition comprises 50-300 mg SNAC, 5-300 mg sodium caprate, 10-80 mg PCSK9 inhibitor, 50-300 mg hydrotrope and 2-8 mg lubricant. In a preferred embodiment, a unit dose of the composition comprises 20-600 mg SNAC, 20-600 mg sodium caprate, 10-80 mg PCSK9 inhibitor, 10-600 mg nicotinamide and 0.10-50 mg magnesium stearate. In a preferred embodiment, a unit dose of the composition comprises 30-500 mg SNAC, 30-500 mg sodium caprate, 10-50 mg PCSK9 inhibitor,10-600 mg nicotinamide and 0.10-25 mg magnesium stearate. In a preferred embodiment, a unit dose of the composition comprises 50-300 mg SNAC, 5-300 mg sodium caprate, 10-80 mg PCSK9 inhibitor, 50-300 mg nicotinamide and 2-8 mg magnesium stearate. In a preferred embodiment, a unit dose of the composition comprises 90-250 mg SNAC, 90-250 mg sodium caprate, 10-80 mg PCSK9 inhibitor, 50-170 mg nicotinamide and 3-7 mg magnesium stearate. In one embodiment, the composition comprises: i) 0.1-200 mg PCSK9 inhibitor, ii) 25-1000 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 15-750 mg, such as 50-200 mg, nicotinamide or resorcinol, iv) 25-1000 mg of a medium chain fatty acid consisting of 6-14 carbon atoms, such capric acid, or a salt hereof such as sodium caprate, and v) 0-50 mg lubricant. In one embodiment, the composition comprises: i) 0.1-150 mg PCSK9 inhibitor, ii) 25-1000 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 15-750 mg, such as 50-200 mg, nicotinamide or resorcinol, iv) 25-1000 mg of a medium chain fatty acid consisting of 6-14 carbon atoms, such capric acid, or a salt hereof such as sodium caprate, and v) 0-25 mg lubricant. In one embodiment, the composition comprises: i) 1-100 mg PCSK9 inhibitor, ii) 50-800 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 40-600 mg nicotinamide, iv) 50-800 mg of a medium chain fatty acid consisting of 6-14 carbon atoms, such capric acid, or a salt hereof such as sodium caprate, and v) 0-20 mg lubricant. In one embodiment, the composition comprises: i) 1-100 mg PCSK9 inhibitor, ii) 50-600 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 40-400 mg nicotinamide, iv) 50-600 mg of a medium chain fatty acid consisting of 6-14 carbon atoms, such capric acid, or a salt hereof such as sodium caprate, and v) 0-15 mg lubricant. In one embodiment, the composition comprises: i) 5-100 mg PCSK9 inhibitor, ii) 55-400 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 45-300 mg nicotinamide, iv) 55-400 mg sodium caprate, and v) 0-10 mg magnesium stearate. In one embodiment, the composition comprises: i) 10-80 mg PCSK9 inhibitor, ii) 150-230 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 100-160 mg nicotinamide, iv) 150-230 mg sodium caprate, and v) 0-10 mg magnesium stearate. In one embodiment, the composition comprises: i) 10-50 mg PCSK9 inhibitor, ii) 100-160 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 65-110 mg nicotinamide, iv) 100-160 mg sodium caprate, and v) 0-10 mg magnesium stearate. In one embodiment, the composition comprises: i) 30-50 mg PCSK9 inhibitor, ii) 125-175 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 80-120 mg nicotinamide, iv) 125-175 mg sodium caprate, and v) 1-8 mg magnesium stearate. In some embodiments the composition may be granulated prior to being compacted and i.e. compressed into tablets. The composition may comprise a granular part (or parts) and/or an extragranular part, wherein the granular part(s) has/have been granulated and the extra-granular part added after granulation. The granular part(s) comprise(s) the two absorption enhancers and the hydrotrope and optionally the therapeutic peptide. In an embodiment the granular part(s) comprise(s) a further excipient, such as a lubricant and/or glidant. In an embodiment the extra-granular part comprises the therapeutic peptide. In an embodiment the extra-granular part comprises a lubricant and/or a glidant, such as magnesium stearate. In an embodiment the extra-granular part comprises the therapeutic peptide and a lubricant and/or a glidant, such as magnesium stearate. Preparation of solid pharmaceutical compositions for oral administration Preparation of a composition according to the invention may be performed according to methods known in the art. To prepare a dry blend of tabletting material, the various components are optionally delumped or sieved, weighed, and then combined. The mixing of the components may be carried out until a homogeneous blend is obtained. The terms “granulate” and “granules” are used interchangeably herein to refer to particles of composition material which may be prepared as described above. The term refers broadly to pharmaceutical ingredients in the form of particles, granules and aggregates which are used in the preparation of solid dose formulations. Generally, granules are obtained by processing a powder or a blend to obtain a solid which is subsequently broken down to obtain granules of the desired size. If granules are to be used in the tabletting material, granules may be produced in a manner known to a person skilled in the art, for example using wet granulation methods known for the production of "built-up" granules or "broken-down" granules. Methods for the formation of built-up granules may operate continuously and comprise, for example simultaneously spraying the granulation mass with granulation solution and drying, for example in a drum granulator, in pan granulators, on disc granulators, in a fluidized bed, by spray-drying, spray-granulation or spray-solidifying, or operate discontinuously, for example in a fluidized bed, in a rotary fluid bed, in a batch mixer, such as a high shear mixer or a low shear mixer, or in a spray-drying drum. Methods for the production of broken-down granules, which may be carried out discontinuously and in which the granulation mass first forms a wet aggregate with the granulation solution, which is subsequently comminuted or by other means formed into granules of the desired size and the granules may then be dried. Suitable equipment for the wet granulation step is, but not limited to, planetary mixers, low shear mixers, high shear mixers, extruders and spheronizers, such as an apparatus from the companies Loedige, Glatt, Diosna, Fielder, Collette, Aeschbach, Alexanderwerk, Ytron, Wyss & Probst, Werner & Pfleiderer, HKD, Loser, Fuji, Nica, Caleva and Gabler. Granules may also be formed by dry granulation techniques in which one or more of the excipient(s) and/or an active pharmaceutical ingredient, such as a peptide therapeutic as described herein, is compressed to form relatively large moldings, for example slugs or ribbons, which are comminuted by grinding, and the ground material serves as the tabletting material to be later compacted. Suitable equipment for dry granulation is, but not limited to, roller compaction equipment from Gerteis such as Gerteis MICRO-PACTOR, MINI-PACTOR and MACRO- PACTOR. Granules may alternatively be prepared by hot melt extruding techniques in which one or more of the excipient(s) is feed into an extruder, heated and extruded through a die. Suitable equipment is such as Thermo Scientific Process 11 twin screw. To compact the tabletting material into a solid oral dosage form, for example a tablet, a tablet press may be used. In a tablet press, the tabletting material is filled (e.g. force feeding or gravity feeding) into a die cavity. The tabletting material is then compacted by a set of punches applying pressure. Subsequently, the resulting compact, or tablet is ejected from the tablet press. The above-mentioned tabletting process is subsequently referred to herein as the "compaction process". Suitable tablet presses include, but are not limited to, rotary tablet presses and eccentric tablet presses. Examples of tablet presses include, but are not limited to, the Fette 102i (Fette GmbH), the Korsch XL100, the Korsch PH 106 rotary tablet press (Korsch AG, Germany), the Korsch EK-O eccentric tabletting press (Korsch AG, Germany) and the Manesty F-Press (Manesty Machines Ltd., United Kingdom). In general, granulates may be prepared by extrusion, wet or dry granulation. Granules comprising one or more of the two absorption enhancers and nicotinamide may thus be obtained by dry granulation, such as by roller compaction. In an alternative embodiment wet granulation may be used to obtain the granules. In an alternative embodiment hot melt extrusion may be used to obtain the granules. The ingredients of a pharmaceutical composition according to the invention may thus be mix or blended prior or after granulation. The granulates can then be used directly or further refined to obtain the final granules. In an embodiment the composition comprises at least one granulate. In an embodiment the composition comprises one type of granulate. The composition may alternatively comprise two types of granulates. In embodiments where the granular part comprises both the absorption enhancers and the hydrotrope these excipients may be co-processed prior to or in the preparation of the granules. The granulation maybe be obtained by various methods as described above, wherein the excipients are initially mixed either as powders or by the preparation of a solution comprising the ingredients. In an alternative embodiment, granules of the excipients are obtained by feeding all ingredients separately into the process stream, such as into an extruder or a compactor. Granules may then be obtained by dry granulation of the blend, such as by roller compaction. In an alternative embodiment the excipients may be hot melt extruded to obtain an extrudate which is optionally subsequently milled to obtain the granules. This material can then be used directly or in dry granulation/roller compaction process to obtain the final granules. In one embodiment a solution of the excipient(s) is prepared and subject to spray granulation whereby granules are directly obtained. Alternatively, the solution can be used in a fluid bed spray granulation process. In one embodiment spray drying can be used followed by dry granulation/roller compaction to obtain granules. In one embodiment a solution of the excipient(s) is prepared, and granules prepared by wet granulation. In one embodiment different processes may be used for different excipient(s). The peptide therapeutic may be included at any step in the process except in the hot melt extrusion. In one embodiment the peptide therapeutic is included in the blend prior to dry granulation or wet granulation. In one embodiment the peptide therapeutic agonist is comprised by a granule produced by dry granulation, such as roller compaction. In one embodiment the peptide therapeutic is comprised by a granule produced by wet granulation. In one embodiment the peptide therapeutic is added after granulation. In one embodiment the invention relates to a method of preparation a solid pharmaceutical composition according to the invention. In one embodiment the method of preparing a tablet comprises the steps of: a) granulating the absorption enhancers and a hydrotrope b) blending the granulates of a) with a peptide therapeutic, and optionally a lubricant c) compressing the blend of b) into tablets. In one embodiment the method of preparing a tablet comprises the steps of: a) granulating a peptide therapeutic, the absorption enhancers and a hydrotrope b) optionally blending of the granulate of a) with a lubricant c) compressing the granules of a) or the blend of b) into tablets. The granulation may be a wet, hot or dry granulation. As described above a lubricant, such as magnesium stearate or glyceryl behenate may be included in any of the steps. In one embodiment the invention relates to a method for producing a solid pharmaceutical composition comprising the steps of: a) obtaining a salt of NAC and a hydrotrope, b) co-processing said salt of NAC and hydrotrope of a), c) obtaining a salt of capric acid d) blending the product of b) with the salt of capric acid of c) and e) optionally include a lubricant in the blending process d) f) preparing said solid pharmaceutical composition using the blend of d) or e) wherein a peptide therapeutic is included in any of the steps. In one embodiment a GLP-1 agonist is included in blending step d) or e) or in a separate blending step. In one embodiment the method is for producing a solid pharmaceutical composition comprising a peptide therapeutic, wherein the method comprises the steps of: a) obtaining a salt of NAC and a hydrotrope, b) hot melt extruding said salt of NAC and hydrotrope of a) and c) obtaining a salt of capric acid d) granulating the salt of capric acid e) blending the product of b) with the granulate of d) and f) optionally include a lubricant in the blending process e) g) preparing said solid pharmaceutical composition using the blend of e) or f) wherein the GLP-1 agonist is included in any of the steps. In one embodiment the peptide therapeutic is included in the granules prepared in d), the blending step e) or f) or in a separate blending step. The method may as described herein include further steps, such as a step of admixing the extrudate of b) with an active pharmaceutical ingredient and optionally any further excipients and preparing said solid pharmaceutical composition using the mixture. Pharmaceutical Indications The present invention relates to a composition comprising a peptide therapeutic, such as a GLP-1 peptide agonist for use as a medicament. In particular embodiments the composition may be used for the following medical treatments, all preferably relating one way or the other to diabetes: (i) prevention and/or treatment of all forms of diabetes, such as hyperglycemia, type 2 diabetes, impaired glucose tolerance, type 1 diabetes, non-insulin dependent diabetes, MODY (maturity onset diabetes of the young), gestational diabetes, and/or for reduction of HbA1C; (ii) delaying or preventing diabetic disease progression, such as progression in type 2 diabetes, delaying the progression of impaired glucose tolerance (IGT) to insulin requiring type 2 diabetes, and/or delaying the progression of non-insulin requiring type 2 diabetes to insulin requiring type 2 diabetes; (iii) improving β-cell function, such as decreasing β-cell apoptosis, increasing β-cell function and/or β-cell mass, and/or for restoring glucose sensitivity to β-cells; (iv) prevention and/or treatment of cognitive disorders; (v) prevention and/or treatment of eating disorders, such as obesity, e.g. by decreasing food intake, reducing body weight, suppressing appetite, inducing satiety; treating or preventing binge eating disorder, bulimia nervosa, and/or obesity induced by administration of an antipsychotic or a steroid; reduction of gastric motility; and/or delaying gastric emptying; (vi) prevention and/or treatment of diabetic complications, such as neuropathy, including peripheral neuropathy; nephropathy; or retinopathy; (vii) improving lipid parameters, such as prevention and/or treatment of dyslipidemia, lowering total serum lipids; lowering HDL; lowering small, dense LDL; lowering VLDL: lowering triglycerides; lowering cholesterol; increasing HDL; lowering plasma levels of lipoprotein a (Lp(a)) in a human; inhibiting generation of apolipoprotein a (apo(a)) in vitro and/or in vivo; (iix) prevention and/or treatment of cardiovascular diseases, such as syndrome X; atherosclerosis; myocardial infarction; coronary heart disease; stroke, cerebral ischemia; an early cardiac or early cardiovascular disease, such as left ventricular hypertrophy; coronary artery disease; essential hypertension; acute hypertensive emergency; cardiomyopathy; heart insufficiency; exercise tolerance; chronic heart failure; arrhythmia; cardiac dysrhythmia; syncopy; atheroschlerosis; mild chronic heart failure; angina pectoris; cardiac bypass reocclusion; intermittent claudication (atheroschlerosis oblitterens); diastolic dysfunction; and/or systolic dysfunction; (ix) prevention and/or treatment of gastrointestinal diseases, such as inflammatory bowel syndrome; small bowel syndrome, or Crohn’s disease; dyspepsia; and/or gastric ulcers; (x) prevention and/or treatment of critical illness, such as treatment of a critically ill patient, a critical illness poly-nephropathy (CIPNP) patient, and/or a potential CIPNP patient; prevention of critical illness or development of CIPNP; prevention, treatment and/or cure of systemic inflammatory response syndrome (SIRS) in a patient; and/or for the prevention or reduction of the likelihood of a patient suffering from bacteraemia, septicaemia, and/or septic shock during hospitalisation; and/or (xi) prevention and/or treatment of polycystic ovary syndrome (PCOS). In a particular embodiment, the indication is selected from the group consisting of (i)-(iii) and (v)-(iix), such as indications (i), (ii), and/or (iii); or indication (v), indication (vi), indication (vii), and/or indication (iix). In another particular embodiment, the indication is (i). In a further particular embodiment the indication is (v). In a still further particular embodiment the indication is (iix). In some embodiments the indications are type 2 diabetes and/or obesity. The invention further relates to a method of treatment of an individual in need thereof, comprising administering a therapeutically active amount of a composition comprising a peptide therapeutics, such as GLP-1 agonist according to the present invention to said individual. In a further such embodiments one or more dose units may be administered to said individual in need. In one aspect the invention relates to the use of a solid composition comprising a PCSK9 inhibitor, such as an EGF(A) peptide analogue or an EGF(A) derivative for use in the manufacture of a pharmaceutical composition as described herein. In one aspect the invention relates to a solid composition comprising a PCSK9 inhibitor, such as an EGF(A) peptide analogue or an EGF(A) derivative, for use as a medicament and/or in a method of treatment. In one embodiment, the composition is for use in a method of treatment, such as for (i) improving lipid parameters, such as prevention and/or treatment of dyslipidaemia, lowering total serum lipids; lowering LDL-C, increasing HDL; lowering small, dense LDL; lowering VLDL; lowering triglycerides; lowering cholesterol; lowering plasma levels of lipoprotein a (Lp(a)); inhibiting generation of apolipoprotein A (apo(A)) ; (ii) the prevention and/or the treatment of cardiovascular diseases, such as cardiac syndrome X, atherosclerosis, myocardial infarction, coronary heart disease, reperfusion injury, stroke, cerebral ischemia, an early cardiac or early cardiovascular disease, left ventricular hypertrophy, coronary artery disease, hypertension, essential hypertension, acute hypertensive emergency, cardiomyopathy, heart insufficiency, exercise intolerance, acute and/or chronic heart failure, arrhythmia, cardiac dysrhythmia, syncopy, angina pectoris, cardiac bypass and/or stent reocclusion, intermittent claudication (atheroschlerosis oblitterens), diastolic dysfunction, and/or systolic dysfunction; and/or the reduction of blood pressure, such as reduction of systolic blood pressure; the treatment of cardiovascular disease. Dyslipidaemia may be such as a high plasm concentration of cholesterols also called hypercholesterolaemia referring to a situation where the plasma cholesterol concentrations is above the normal range of a total cholesterol ≥ 5.0 mmol/l. In one embodiment, the compound or composition of the invention may be used for treatment of hypercholesterolaemia. Method of treatment The invention further relates to a method of treating a subject in need thereof, comprising administering a therapeutically effective amount of a composition according to the present invention to said subject. In one embodiment, where the peptide therapeutic is a GLP-1 agonist, the method is for treatment of a disease or disorder, such as diabetes and/or obesity and/or the further indications specified above. In some embodiments, a method for treating a disease or disorder, such as diabetes and/or obesity comprises administering to a subject in need thereof a therapeutically effective amount of a pharmaceutical composition comprising a therapeutic peptide, such a GLP-1 agonist, a salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), a hydrotrope, a second absorption enhancer and optionally, a lubricant. In some embodiments, the method for treating a disease or disorder, comprises administering to a subject in need thereof a therapeutically effective amount of a pharmaceutical composition comprising i) 0.1-100 mg therapeutic peptide ii) 20-1000 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC) iii) 20-1000 mg of a fatty acid consisting of 6-14 carbon atoms, such as capric acid, or a salt hereof, such as sodium caprate iv) 10-500 mg nicotinamide and v) 0-25 mg lubricant. In some embodiments, the therapeutic peptide is a GLP-1 agonist such as semaglutide having a formula of N-epsilon26-[2-(2-{2-[2-(2-{2-[(S)-4-carboxy-4-(17-carboxy- heptadecanoylamino)butyrylamino]ethoxy}ethoxy)acetylamino]et hoxy}ethoxy)acetyl] [Aib8,Arg34]GLP-1(7-37) and the salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC) is sodium N-(8-(2-hydroxybenzoyl)amino)caprylic acid (SNAC). In some embodiments, the therapeutic peptide is a GLP-1 agonist such as diacylated [Aib8,Arg34,Lys37]GLP-1(7-37) (SEQ ID NO.4) and named N ^ε26 {2-[2-(2-{2-[2-(2-{(S)-4-Carboxy- 4-[10-(4-carboxyphenoxy)decanoylamino]butyrylamino}- ethoxy)ethoxy]acetylamino}ethoxy)ethoxy]acetyl}, N ^ε37 -{2-[2-(2-{2-[2-(2-{(S)-4-carboxy-4-[10-(4- carboxyphenoxy)decanoylamino]butyrylamino}ethoxy)ethoxy]acet ylamino}ethoxy)ethoxy]-acetyl}- [Aib ⁸ ,Arg ³⁴ ,Lys ³⁷ ]GLP-1(7-37)–peptide (GLP-1 peptide 1). In some embodiments, the GLP-1 agonist is N ^ε27 -[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4- [10-(4-carboxyphenoxy)decanoylamino]butanoyl]amino] ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy]-acetyl], N ^ε36 -[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-[10- (4-carboxyphenoxy)decanoylamino]- butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy]acet yl]-[Aib8,Glu22,Arg26,Lys27, Glu30,Arg34,Lys36]-GLP-1-(7-37)-peptidyl-Glu-Gly (GLP-1 peptide 3, SEQ ID No.: 5). In one embodiment the therapeutic peptide is a PCSK9 inhibitor peptide. The invention further relates to a method of treating a subject in need thereof, comprising administering a therapeutically effective amount of a composition according to the present invention to said subject. In one embodiment, the method of treatment is for treatment of a disease or disorder, such as (i) improving lipid parameters and/or (ii) preventing and/or treating cardiovascular diseases and/or the further indications specified above. In some embodiments, a method for treating a disease or disorder, such as (i) improving lipid parameters and/or (ii) preventing and/or treating cardiovascular diseases is described comprising administering to a subject in need thereof a therapeutically effective amount of a pharmaceutical composition comprising a PCSK9 inhibitor, a salt of N-(8-(2- hydroxybenzoyl)amino)caprylic acid (NAC), a hydrotrope, a second absorption enhancer and optionally, a lubricant. In some embodiments, a method for i) improving lipid parameters and/or ii) treating or preventing cardiovascular diseases is described comprising administering to a subject in need thereof a therapeutically effective amount of a pharmaceutical composition comprising i) 0.1-150 mg of a PCSK9 inhibitor, ii) 25-1000 mg of salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt (SNAC), iii) 15-750 mg nicotinamide, iv) 25-1000 mg of a medium chain fatty acid consisting of 6-14 carbon atoms, such as capric acid, or a salt hereof, such as sodium caprate, and v) 0-25 mg lubricant. In some embodiments, the PCSK9 inhibitor is selected from compounds A to J described herein above. In some embodiments, the PCSK9 inhibitor is selected from compounds A, L, C, D, E, F, G H, I and J described herein above. In some embodiments, the PCSK9 inhibitor is compound H disclosed above having the following structure: Various examples of a lubricant are described, including magnesium stearate. The composition is administered orally and is in a form of a table, capsule or a sachet. In a further such embodiments one or more dose units may be administered to said subject in need. In one embodiment a unit dose is administered orally. Combination treatment The treatment with a GLP-1 peptide composition according to the present invention may also be combined with one or more additional active pharmaceutical ingredient(s), e.g. selected from antidiabetic agents, anti-obesity agents, appetite regulating agents, antihypertensive agents, agents for the treatment and/or prevention of complications resulting from or associated with diabetes and agents for the treatment and/or prevention of complications and disorders resulting from or associated with obesity. Examples of these pharmacologically active substances are: Insulin, sulphonylureas, biguanides, meglitinides, glucosidase inhibitors, glucagon antagonists, DPP-IV (dipeptidyl peptidase-IV) inhibitors, sodium glucose linked transporter 2 (SGLT2) inhibitors; canagliflozin, dapagliflozin, empagliflozin, ertugliflozin, ipragliflozin, tofogliflozin, luseogliflozin, bexagliflozin, remogliflozin etabonate and sotagliflozin, particulally dapagliflozin and empagliflozin, inhibitors of hepatic enzymes involved in stimulation of gluconeogenesis and/or glycogenolysis, glucose uptake modulators, compounds modifying the lipid metabolism such as antihyperlipidemic agents as HMG CoA inhibitors (statins), Gastric Inhibitory Polypeptides (GIP analogues), compounds lowering food intake, RXR agonists and agents acting on the ATP-dependent potassium channel of the β-cells; Cholestyramine, colestipol, clofibrate, gemfibrozil, lovastatin, pravastatin, simvastatin, probucol, dextrothyroxine, neteglinide, repaglinide; ^-blockers such as alprenolol, atenolol, timolol, pindolol, propranolol and metoprolol, ACE (angiotensin converting enzyme) inhibitors such as benazepril, captopril, enalapril, fosinopril, lisinopril, alatriopril, quinapril and ramipril, calcium channel blockers such as nifedipine, felodipine, nicardipine, isradipine, nimodipine, diltiazem and verapamil, and α-blockers such as doxazosin, urapidil, prazosin and terazosin; CART (cocaine amphetamine regulated transcript) agonists, NPY (neuropeptide Y) antagonists, PYY agonists, Y2 receptor agonists, Y4 receptor agonists, mixed Y2/Y4 receptor agonists, MC4 (melanocortin 4) agonists, orexin antagonists, TNF (tumour necrosis factor) agonists, CRF (corticotropin releasing factor) agonists, CRF BP (corticotropin releasing factor binding protein) antagonists, urocortin agonists, β3 agonists, oxyntomodulin and analogues, MSH (melanocyte-stimulating hormone) agonists, MCH (melanocyte-concentrating hormone) antagonists, CCK (cholecystokinin) agonists, serotonin re- uptake inhibitors, serotonin and noradrenaline re-uptake inhibitors, mixed serotonin and noradrenergic compounds, 5HT (serotonin) agonists, bombesin agonists, galanin antagonists, growth hormone, growth hormone releasing compounds, TRH (thyreotropin releasing hormone) agonists, UCP 2 or 3 (uncoupling protein 2 or 3) modulators, leptin agonists, DA agonists (bromocriptin, doprexin), lipase/amylase inhibitors, RXR (retinoid X receptor) modulators, TR ^ agonists; histamine H3 antagonists, Gastric Inhibitory Polypeptide agonists or antagonists (GIP analogues), gastrin and gastrin analogues. Treatment with a PCSK9 inhibitor in a composition according to the present invention may be combined with treatment with one or more additional pharmacologically active substances, e.g. selected from anti-diabetic agents, anti-obesity agents, appetite regulating agents, antihypertensive agents, agents for the treatment and/or prevention of complications resulting from or associated with diabetes and agents for the treatment and/or prevention of complications and disorders resulting from or associated with obesity. Examples of such pharmacologically active substances are: GLP-1 receptor agonists, insulin, DPP-IV (dipeptidyl peptidase-IV) inhibitors, amylin agonists, anti-inflammatory, triglyceride-lowering agents and leptin receptor agonists. Particular examples of such active substances are the GLP-1 receptor agonists liraglutide and semaglutide. EMBODIMENTS 1. A solid pharmaceutical composition comprising a) a therapeutic peptide of at least 20 amino acid residues b) a salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), c) a fatty acid consisting of 6-14 carbon atoms or a salt hereof and d) hydrotrope. 2. The composition according to embodiment 1, wherein the therapeutic peptide is at least 30, such as at least 40, such as at least 50 amino acid residues. 3. The composition according to any of the previous embodiments, wherein the peptide therapeutic comprises 20-500 amino acids residues. 4. The composition according to any of the previous embodiments, wherein the peptide therapeutic comprises one or more modified amino acid residue and/or non-proteogenic amino acid residues. 5. The composition according to any of the previous embodiments, wherein the peptide therapeutic has an extended half-life. 6. The composition according to any of the previous embodiments, wherein the peptide therapeutic has a plasma half-life in humans of at least 24 hours, such as at least 48 hours, such as at least 72 hours. 7. The composition according to any of the previous embodiments, wherein the peptide therapeutic has a plasma half-life in humans of at least 96 hours, such as 120-200 hours, 8. The composition according to any of the previous embodiments, wherein the therapeutic peptide is a fatty acid substituted peptide. 9. The composition according to any of the previous embodiments, wherein the therapeutic peptide has an albumin binding substituent. 10. The composition according to any of the previous embodiments, wherein the peptide therapeutic comprises an albumin binding moiety. 11. The composition according to any of the previous embodiments, wherein the peptide therapeutic comprises two albumin binding moieties. 12. The composition according to any of the previous embodiments, wherein the peptide therapeutic comprises a substituent comprising an albumin binding moiety. 13. The composition according to any of the previous embodiments, wherein the peptide therapeutic comprises two substituents comprising an albumin binding moiety. 14. The composition according to any of the previous embodiments, wherein the substituent comprising an albumin binding moiety is attached via a lysine residue. 15. The composition according to any of the previous embodiments, wherein the substituent comprising an albumin binding moiety is attached via an epsilon nitrogen of a lysine residue. 16. The composition according to any of the previous embodiments, wherein the albumin binding moiety is selected from the group consisting of: Chem.1: HOOC-(CH2)n-CO-* wherein n is an integer in the range of 8-20, Chem.2: 5-tetrazolyl-(CH2)n-CO-* wherein n is an integer in the range of 8-20, Chem.3: HOOC-(C6H4)-O-(CH2)m-CO-* wherein n is an integer in the range of 8-20, Chem.4: HO-S(O)2-(CH2)n-CO-* wherein n is an integer in the range of 8-20, Chem.5: MeS(O)2NH(CO)NH-(CH2)n-CO-* wherein n is an integer in the range of 8-20 and Chem.6: 3-HO-Isoxazole-(CH2)n-CO-* wherein n is an integer in the range of 8-20 wherein the symbol * indicates the attachment point to a linker or the peptide. 17. The composition according to any of the previous embodiments, wherein the substituent comprises a linker. 18. The composition according to any of the previous embodiments, wherein the linker comprises one or more elements selected from the group consisting of: Glu, γGlu, Gly, Ser, Ala, Thr, Ado, Aeep, Aeeep and TtdSuc. 19. The composition according to embodiment 1-4, wherein the therapeutic peptide is a GLP- 1 agonist. 20. The composition according to embodiment 1-5, wherein the therapeutic peptide is a GLP- 1 receptor agonist. 21. The composition according to embodiment 1, wherein the therapeutic peptide is semaglutide. 22. The composition according to embodiment 1, wherein the therapeutic peptide is GLP-1 peptide 1 or GLP-1 peptide 3. 23. The composition according to embodiment 1, wherein the therapeutic peptide is a pro- drug of semaglutide. 24. The composition according to embodiment 1, wherein the therapeutic peptide is an insulin analogue. 25. The composition according to embodiment 1, wherein the therapeutic peptide is a PCSK9 inhibitor. 26. The composition according to embodiment 1, wherein the therapeutic peptide is a PCSK9 inhibitor peptide selected from the group consisting of:

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27. The composition according to any of the previous embodiments, wherein the peptide therapeutic is a PCSK9 inhibitor peptide selected from the group consisting of compounds G, H, I and J. 28. The composition according to any of the previous embodiments, wherein the peptide therapeutic is compound H 29. The composition according to any of the previous embodiments, wherein the hydrotrope is selected from the group consisting of : Resorcinol, Pyrocatechol, Pyrogallol, Gentisic acid, Xylenesulfonate, p-toluenesulfonate, Nicotinamide, Dimethylbenzamide, Diethylbenzamide, 1-methylnicotinamide, Salicyclic acid and P-Hydroxybenzoic acid. 30. The composition according to any of the previous embodiments, wherein the hydrotrope is nicotinamide and/or Resorcinol. 31. The composition according to any of the previous embodiments, wherein the hydrotrope is nicotinamide. 32. The composition according to any of the previous embodiments, wherein the hydrotrope is not sodium benzoate. 33. The composition according to any of the previous embodiments, wherein the composition further comprises a lubricant. 34. The composition according to embodiment 13, wherein the lubricant is magnesium stearate or glyceryl dibehenate. 35. The composition according to embodiment 13, wherein the lubricant is magnesium stearate 36. The composition according to any of the previous embodiments, wherein the fatty acid is a saturated fatty acid. 37. The composition according to any of the previous embodiments, wherein the fatty acid is consisting of 8-12 carbon atoms or 10-12 carbon atoms. 38. The composition according to any of the previous embodiments, wherein the fatty acid is capric acid or a salt thereof. 39. The composition according to any of the previous embodiments, wherein the fatty acid or a salt hereof is sodium caprate. 40. The composition according to any of the previous embodiments, wherein the salt of NAC is selected form the sodium, the potassium and the ammonium salt of NAC. 41. The composition according to any of the previous embodiments, wherein the salt of NAC is sodium N-(8-(2-hydroxybenzoyl)amino)caprylate (SNAC). 42. The composition according to any one of the preceding embodiments, wherein the weight ratio (w/w) of the amount (w) of salt of NAC and the amount (w) of the hydrotrope is at least 0.5. 43. The composition according to any of the previous embodiments, wherein the weight ratio (w/w) of the amount (w) of salt of NAC and the amount (w) of the hydrotrope is 0.5-10, such as 0.5-8 or such as 0.5-5. 44. The composition according to any of the previous embodiments, wherein the weight ratio (w/w) of the amount (w) of the salt of NAC to the amount (w) of nicotinamide is 0.5-10, such as 0.5-8 or such as 0.5-5. 45. The composition according to any of the previous embodiments, wherein the weight ratio (w/w) of the amount (w) of SNAC to the amount (w) of nicotinamide is 0.5-5, such as 0.8- 3 or such as 0.5-5. 46. The composition according to any of the previous embodiments, wherein the weight ratio (w/w) of the amount (w) of salt of NAC to the amount (w) of hydrotrope is 0.5-2, such as 1-2, or such as 1.2-1.8. 47. The composition according to any of the previous embodiments, wherein the weight ratio (w/w) of the amount (w) of salt of NAC to the amount (w) of nicotinamide is 0.5-2, such as 1-2, or such as 1.2-1.8. 48. The composition according to any of the previous embodiments, wherein the weight ratio (w/w) of the amount (w) of SNAC to the amount (w) of nicotinamide is 0.5-2, such as 1-2, or such as 1.2-1.8 49. The composition according to any of the previous embodiments, wherein the weight ratio (w/w) of the amount (w) of salt of NAC to the amount (w) of hydrotrope is 1-2, such as 1.2-1.8 or such as 1.3-1.7, or such as 1.4-1.6. 50. The composition according to any of the previous embodiments, wherein the weight ratio (w/w) of the amount (w) of salt of NAC to the amount (w) of nicotinamide is 1-2, such as 1.2-1.8 or such as 1.3-1.7, or such as 1.4-1.6. 51. The composition according to any of the previous embodiments, wherein the weight ratio (w/w) of the amount (w) of SNAC to the amount (w) of nicotinamide is 1-2, such as 1.2- 1.8 or such as 1.3-1.7, or such as 1.4-1.6. 52. The composition according to any of the previous embodiments, wherein the weight ratio (w/w) of the amount (w) of the salt of NAC to the of the amount (w) of the fatty acid or salt hereof is 0.5-10, such as 0.5-5 or such as 0.5-2. 53. The composition according to any of the previous embodiments, wherein the weight ratio (w/w) of the amount (w) of the salt of NAC and the amount (w) of capric acid or a salt hereof is 0.5-10, such as 0.5-5 or such as 0.5-2. 54. The composition according to any of the previous embodiments, wherein the weight ratio (w/w) of the amount (w) of the salt of NAC and the amount (w) of sodium caprate is 0.5- 10, such as 0.5-5 or such as 0.5-2. 55. The composition according to any of the previous embodiments, wherein the weight ratio (w/w) of the amount (w) of SNAC to the amount (w) of sodium caprate is 0,5-10, such as 0.5-5 or such as 0.5-2. 56. The composition according to any one of the preceding embodiments, wherein the ratio of salt of NAC/medium chain fatty acid or salt thereof is 0.5-2, such as 0.8-1.7 or such as 0.9-1.2. 57. The composition according to any one of the preceding embodiments, wherein the ratio of SNAC/capric acid or salt thereof is 0.5-2, such as 0.8-1.7 or such as 0.9-1.2. 58. The composition according to any one of the preceding embodiments, wherein the ratio of SNAC/sodium caprate is 0.3-3, such as 0.4-2.5 or such as 0.5-2. 59. The composition according to any one of the preceding embodiments, wherein the ratio of SNAC/sodium caprate is 0.5-2, such as 0.8-1.7 or such as 0.9-1.2. 60. The composition according to any of the previous embodiments consisting of: a) a therapeutic peptide of at least 10, such as at least 20 amino acid residues, b) a salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), c) a fatty acid consisting of 6-14 carbon atoms, such capric acid, or a salt hereof, such as sodium caprate, d) nicotinamide or resorcinol and e) a lubricant. 61. The composition according to any of the previous embodiments, wherein the composition comprises 1-100 mg of the peptide therapeutic. 62. The composition according to any of the previous embodiments, wherein the composition comprises 1-50, 1-40 mg, 1-30 mg, 1-25, or 1-20 mg of the peptide therapeutic. 63. The composition according to any of the previous embodiments, wherein the composition comprises 10-100, 20-100 mg, 30-100 mg, 40-100 or 50-100 mg of the peptide therapeutic. 64. The composition according to any of the previous embodiments, wherein the amount of the peptide therapeutic is less than 50 % w/w, such as less than 40, 30, 20, 15, 10 or 5 % w/w of the composition. 65. The composition according to any of the previous embodiments, wherein a unit dosage comprises 0.1-100 mg of a GLP-1 agonist. 66. The composition according to any of the previous embodiments, wherein a unit dosage comprises 1-100 mg semaglutide. 67. The composition according to any one of the previous embodiments, wherein a unit dose comprises 0.1-200 mg of a PCSK9 inhibitor. 68. The composition according to any one of the preceding embodiments, wherein a unit dose comprises 1-100 mg of the PCSK9 inhibitor Compound H having the structure: 69. The composition according to any of the previous embodiments, wherein a unit dosage comprises at most 1000 mg of said salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC). 70. The composition according to any of the previous embodiments, wherein a unit dosage comprises at least 20 mg of said salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC). 71. The composition according to any of the previous embodiments, wherein a unit dosage comprises 20-1000 mg of said salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC). 72. The composition according to any of the previous embodiments, wherein a unit dosage comprises at most 1000 mg of said fatty acid or salt thereof, such as said salt of capric acid. 73. The composition according to any of the previous embodiments, wherein a unit dosage comprises at least 20 mg of said fatty acid or salt thereof, such as said salt of capric acid. 74. The composition according to any of the previous embodiments, wherein a unit dosage comprises 20-1000 mg of said fatty acid or salt thereof, such as said salt of capric acid. 75. The composition according to any of the previous embodiments, wherein a unit dosage comprises 10-600 mg of the hydrotrope, such as nicotinamide. 76. The composition according to any of the previous embodiments, wherein a unit dosage comprises 0.1-25 mg lubricant, such as magnesium stearate. 77. The composition according to any of the previous embodiments, wherein a unit dosage comprises i) 0.1-100 mg therapeutic peptide of at least 20 amino acid residues, ii) 200-1000 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 20-1000 mg of a fatty acid consisting of 6-14 carbon atoms, such as capric acid, or a salt hereof, such as sodium caprate, iv) 10-500 mg nicotinamide and v) 0-25 mg lubricant. 78. The composition according to any of the previous embodiments, wherein a unit dosage comprises vi) 0.5-100 mg GLP-1 agonist, vii) 20-1000 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), viii) 20-1000 mg a fatty acid consisting of 6-14 carbon atoms, such capric acid, or a salt hereof such as sodium caprate ix) 10-750 mg, such as 50-200 mg nicotinamide or resorcinol and x) 0-25 mg lubricant. 79. The composition according to any of the previous embodiments, wherein a unit dosage comprises i) 1-75 mg GLP-1 agonist, ii) 25-300 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), iii) 25-300 mg a fatty acid consisting of 6-14 carbon atoms, such capric acid, or a salt hereof such as sodium caprate, iv) 15-200 mg nicotinamide and v) 0-10 mg lubricant. 80. The composition according to any of the previous embodiments, wherein a unit dosage comprises: a) 1-75 mg GLP-1 agonist, b) 20-200 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), c) 20-200 mg sodium caprate, d) 10-150 mg nicotinamide and e) 0-10 mg magnesium stearate. 81. The composition according to any of the previous embodiments, wherein a unit dosage comprises a) 1-50 mg GLP-1 agonist, b) 20-100 mg salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid (NAC), such as the sodium salt of NAC (SNAC), c) 20-100 mg sodium caprate, d) 10-75 mg nicotinamide and e) 0-10 mg magnesium stearate. 82. The composition according to any of the previous embodiments, wherein the composition comprises i) 0.1-200 mg of a PCSK9 inhibitor peptide; ii) 20-600 mg, such as 25-400 mg, such as 50-300 mg of a salt of N-(8-(2- hydroxybenzoyl)amino)caprylic acid; iii) 20-600 mg, such as 25-400 mg, such as 50-300 mg of a medium chain fatty acid consisting of 6-14 carbon atoms, such as capric acid or a salt thereof, such as sodium caprate; iv) 10-400 mg Nicotinamide; and v) 0-50 mg lubricant. 83. The composition according to any one of the preceding embodiments, wherein the composition comprises: i) 1-100 mg, such as 5-80 mg of a PCSK9 inhibitor peptide; ii) 50-500 mg of a salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid; iii) 50-500 mg of a saturated, medium-chain fatty acid consisting of 6-14 carbon atoms or a salt thereof; iv) 10-400 mg Nicotinamide; and v) 0-25 mg lubricant. 84. The composition according to any one of the preceding embodiments, wherein the composition comprises: i) 10-80 mg of a PCSK9 inhibitor peptide; ii) 50-400 mg of a salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid; iii) 50-400 mg of a saturated, medium-chain fatty acid consisting of 6-14 carbon atoms or a salt thereof; iv) 10-300 mg Nicotinamide; and v) 0-20 mg lubricant. 85. The composition according to any one of the preceding embodiments, wherein the composition comprises: i) 10-50 mg of a PCSK9 inhibitor peptide; ii) 50-300 mg of a salt of N-(8-(2-hydroxybenzoyl)amino)caprylic acid; iii) 50-300 mg of a saturated, medium-chain fatty acid consisting of 6-14 carbon atoms or a salt thereof; iv) 10-200 mg Nicotinamide; and v) 0-15 mg lubricant. 86. The composition according to any of the previous embodiments wherein the composition is a pharmaceutical composition for oral administration. 87. The composition according to any of the previous embodiments wherein the composition is for use in a method of treatment. 88. The composition according to any of the previous embodiments, wherein the composition is a pharmaceutical composition for use in a method of treating diabetes and/or obesity. 89. A method for treatment of diabetes and/or obesity comprising administering to a subject in need a therapeutically effective amount of a composition according to embodiments 1-81. 90. The method according to embodiment 89, wherein said composition is administered, once daily or less frequent. 91. A method for preparation of a solid pharmaceutical composition comprising the steps of: a) granulating two absorption enhancers and a hydrotrope b) blending the granulates of a) with a therapeutic peptide, such as a GLP-1 peptide or a PCSK9 inhibitor, and optionally a lubricant c) compressing the blend of b) into tablets. 92. A method for preparation of a solid pharmaceutical composition comprising the steps of: a) blending a therapeutic peptide, such as a GLP-1 peptide or a PCSK9 inhibitor, two absorption enhancers, a hydrotrope and optionally a lubricant b) granulating the blend of a) c) optionally blending the granules of a) with a lubricant d) compressing the granules of b) or the blend of c) into tablets. 93. A method for producing a solid pharmaceutical composition comprising the steps of: a) obtaining a salt of NAC and a hydrotrope, b) co-processing said salt of NAC and hydrotrope, c) obtaining a salt of capric acid d) blending the product of b) with the salt of capric acid of c) and e) optionally include a lubricant in the blending process d) f) preparing said solid pharmaceutical composition using the blend of d) or e) wherein a peptide therapeutic, such as a GLP-1 peptide or a PCSK9 inhibitor, is included in any of the steps a)-f). 94. The method according to embodiment 89, wherein a peptide therapeutic, such as a GLP- 1 agonist or a PCSK9 inhibitor is included in blending step d) or e) or in a separate blending step. 95. A method for producing a solid pharmaceutical composition comprising a GLP-1 agonist, wherein the method comprises the steps of: a) obtaining a salt of NAC and a hydrotrope, b) hot melt extruding said salt of NAC and hydrotrope of a) and c) obtaining a salt of capric acid d) granulating the salt of capric acid e) blending the product of b) with the granulate of d) and f) optionally include a lubricant in the blending process e) g) preparing said solid pharmaceutical composition using the blend of e) or f) wherein the GLP-1 agonist is included in any of the steps. 96. The method according to embodiment 95, wherein a GLP-1 agonist is included in the granules prepared in d), the blending step e) or f) or in a separate blending step. 97. A method for producing a solid pharmaceutical composition comprising a PCSK9 inhibitor, wherein the method comprises the steps of: a) obtaining a salt of NAC and a hydrotrope, b) hot melt extruding said salt of NAC and the hydrotrope of a); c) obtaining a salt of capric acid; d) granulating the salt of capric acid; e) blending the product of b) with the granulate of d); and f) optionally include a lubricant in the blending process e); g) preparing said solid pharmaceutical composition using the blend of e) or f) wherein the PCSK9 inhibitor is included in any of the steps. 98. The method according to embodiment 79, wherein a PCSK9 inhibitor is included in the granules prepared in d), the blending step e) or f) or in a separate blending step. 99. The method according to any of the previous embodiments 91-96, wherein the hydrotrope is nicotinamide or Resorcinol. 100. The method according to any of the previous embodiments 91-96, wherein the hydrotrope is nicotinamide. 101. The method according to any of the previous embodiments 91-100, wherein the hydrotrope is not sodium benzoate. 102. The method according to any of the previous embodiments 91-101, wherein the composition further comprises a lubricant. 103. The method according to embodiment 102, wherein the lubricant is magnesium stearate or glyceryl dibehenate. 104. The method according to embodiment 102, wherein the lubricant is magnesium stearate 105. The method according to any of the previous embodiments 91-104, wherein one of the two enhancers are a fatty acid, such as a saturated fatty acid or a salt hereof. 106. The method according to any of the previous embodiments 91-105, wherein the fatty acid is consisting of 8-12 carbon atoms or 10-12 carbon atoms. 107. The method according to any of the previous embodiments 91-105, wherein the fatty acid is capric acid. 108. The method according to any of the previous embodiments 91-105, wherein the fatty acid or a salt hereof is sodium caprate. 109. The method according to any of the previous embodiments 91-108, wherein the salt of NAC is selected form the sodium, the potassium and the ammonium salt of NAC. 110. The method according to any of the previous embodiments 91-108, wherein the salt of NAC is sodium N-(8-(2-hydroxybenzoyl)amino)caprylate (SNAC). EXAMPLES Materials and Methods Assay I: Small volume disintegration test The small volume disintegration test is performed by a vision-based technique capable of accessing semi quantitatively the amount of tablet that has been disintegrated at various time points. During the experiment the tablet is static, and an appropriate small volume of disintegration media is transferred to the tablet. The experiment is conducted at neutral pH in water at 37 °C . Assay II: Pharmacokinetic studies in Beagle dogs Pharmacokinetic (PK) studies in Beagle dogs are conducted to determine the exposure of the therapeutic peptide after peroral administration of different dosage forms. For the pharmacokinetic studies male Beagle dogs are used, 1 to 5 years of age and weighing approximately 10-12 kg at the start of the studies. The dogs are group housed in pens (12 hours light: 12 hours dark) and fed individually and restrictedly once. Exercise and group social are permitted daily, whenever possible. The dogs are used for repeated pharmacokinetic studies with a suitable wash-out period between successive dosing’s. An appropriate acclimatisation period is given prior to initiation of the first pharmacokinetic study. All handling, dosing and blood sampling of the animals are performed by trained and skilled staff. Before the studies the dogs are fasted overnight and from 0 to 4 h after dosing. Besides, the dogs are restricted to water 1 hour before dosing until 4 hours after dosing, but otherwise have ad libitum access to water during the whole period. The tablets used for the per oral studies described herein are immediate release SNAC- based tablets dosed orally. The tablets containing the therapeutic peptide are administered in the following manner: 10 min prior to tablet administration the dogs are dosed subcutaneously with approximately 3.2 nmol/kg (dose volume: 0.011mL/kg) of glucagon. The tablets are placed in the back of the mouth of the dog to prevent chewing. The mouth is then closed, and 10 mL of tap water is given by a syringe to facilitate swallowing of the tablet. Alternatively, 40 mL of water is administered by gavage just prior to tablet dosing, where after the tablet is dosed and 10 mL of tap water is given by a syringe to facilitate swallowing of the tablet. Blood sampling Blood is sampled at predefined time points for up till 10 hr post dosing to adequately cover the full plasma concentration-time absorption profile of the therapeutic peptide For each blood sampling time point approximately 0.8 mL of whole blood is collected in a 1.5 mL EDTA coated tube, and the tube is gently turned to allowing mixing of the sample with the EDTA. Blood samples (for example 0.8 mL) are collected in EDTA buffer (8mM) and then centrifuged at 4°C and 2000G for 10 minutes. Plasma is pipetted into Micronic tubes on dry ice and kept at - 20°C until analysis. Blood samples are taken as appropriate, for example from a venflon in the cephalic vein in the front leg for the first 2 hours and then with syringe from the jugular vein for the rest of the time points (the first few drops are allowed to drain from the venflon to avoid heparin saline from the venflon in the sample). General methods for tablet preparation Method 1: Dry Granulation Prior to dry granulation the enhancer or enhancers is/are blended with magnesium stearate by manual geometric mixing followed by blending on V-shell blender (50 min, 25 rpm). Dry granulation is carried out by roller compaction on a Gerteis MINI-PACTOR. The roller speed is set at 3 rpm and press force of 6 kN/cm and granulated using a star rotor granulation with a wire screen of 0.63 mm. Method 2: Hot melt extrusion Hot melt extrusion is carried out on a Leistritz ZSE Micro 27. The enhancer or enhancers and nicotinamide fed separately into the extruder using gravimetric feeders. The equipment is operated at process temperatures varying between 105˚C to 200˚C along the barrel to facilitate the melt extrusion. The screw speed is approximately 300 rpm. The resulting extrudates are milled using a final screen of 0.4 mm. Method 3 – Wet granulation Twin screw wet granulation is carried out using a Thermo Scientific Process 11 twin screw extruder at a screw speed of 100 rpm. The enhancer is fed into the barrel using a gravimetric feeder at 100 g/h and the granulation medium, water, is added using a peristaltic pump at a rate of 0.25 ml/h. The barrel is water-cooled to 30˚C. Milling of the dried extrudates is carried out using a Frewitt FreDrive-Lab oscillating mill at a speed of 300 mm/s through a 0.355x0.14 mm flat screen. Method 4: Blending for tablet compression Blending is carried out by manual geometric mixing the intermediate granulate with any further ingredients followed by blending on a turbula mixer (7 min, 25 rpm). In compositions including additional magnesium stearate it was sieved through a 125 µm or 355 µm mesh and added in a secondary blending step prior to compression by manual geometric mixing followed by blending on a turbula mixer (2 min, 25 rpm). Method 5: Tablet compression Tablets are produced on a Kilian STYL’One or a Fette 102i mounted with a single set of punches, resulting in either 7 mm round or 6.8 mm × 12 mm or 8 mm x 14 mm oval compound cup tablets having no score. Punch size is chosen according to the total tablet weight. For the Kilian STYL’One the press speed is set to 10% and for Fette 102i the press speed is set at 20 rpm. The fill volume is adjusted to obtain tablets having target weights based on composition. Compression forces around 1 to 25 kN are applied to obtain tablets with a crushing strength of around 20-120 N respective to the tablet size. For the tablet’s compositions described herein the content in weight (mg) of the peptide therapeutic is provided. The peptide therapeutic preparations may include impurities, and thus the absolute weight of peptide therapeutic preparation in a tablet is higher than the listed amount of the peptide therapeutic, and therefore the total weight of the tablet is usually slightly higher than the sum of the ingredients listed. Other methods Detection of GLP-1 analogue and insulin analogue The plasma samples from both humans and dogs were analysed for peptide therapeutic using a Luminescence Oxygen Channeling Immunoassay (LOCI). For GLP-1 analogue analysis, a matched antibody pair (2F6 and 3F15) is involved in the assay, one biotinylated (3F15) and bound to streptavidin-coated Alpha donor beads, and the other conjugated to AlphaLISA acceptor beads (2F6). The binding of the two antibodies to analyte (GLP-1 analogue) brings donor and acceptor beads into proximity, resulting in the excitation of donor beads at 680 nm, triggering chemical reactions in the acceptor beads, and subsequently the emission at 615 nm. This emission signal is measured in the EnVision plate reader for API concentration analysis. The amount of light was proportional to the concentration of active peptide ingredient and the lower limit of quantification (LLOQ) in plasma was 100 pM. For analysing another GLP-1 analogue, the matched antibody pair is 3F15 and 7F1. For insulin analogue analysis, the antibody pair for use is 1F31 and S1C3D3E3. The latter (S1C3D3E3) is biotinylated and bound to streptavidin-coated Alpha donor beads, while the former (1F31) is conjugated to AlphaLISA acceptor beads. Detection of PCSK9i peptide Plasma concentrations of PCSK9i were assayed by plasma protein precipitation and analysed by liquid chromatography-mass spectrometry (LC-MS). Calibrators were prepared by spiking blank plasma with analytes to reach the final concentrations in the range from 2 to 1000 nM. Calibrators, plasma blanks or study samples were prepared for LC-MS by adding 1 volume of 8 M Guanidine-HCl and incubated at 37 °C for 30 minutes. Two and a half volumes of ice-cold methanol containing internal standard were added and mixed on the robot shaker, followed by centrifugation at 4000 rpm at 4°C for 1 h. The supernatant was diluted with 2 volumes of Milli-Q water containing 1% formic acid before injection on the LC-MS system. The system used was a Transcend II Interface Module SRD3200 system from Thermo Scientific (Waltham, MA, USA) coupled to Orbitrap QExactive Plus mass spectrometer from Thermo Scientific. The LC was equipped with a Cyclone column (CH-953288, Thermo Scientific) as the first dimensional trapping column and Aeris 3.6 µm PEPTIDE XB-C18 as the analytical column (2.1 x 50 mm from Phenomenex). The mobile phase composition of the loading pump is as below: mobile phase A consists of 95% milli-Q water, 2.5% acetonitrile, 2.5 % methanol and 1% formic acid; mobile phase B consists of 47.5% acetonitrile, 47.5% methanol, 5% milli-Q water, and 1% formic acid. The analyte of interest was loaded from the Turbo flow column at 15% B to the second dimensional analytical column. The Orbitrap QExactive Plus were operating in positive ionization mode with the parallel reaction monitoring (PRM) scan mode. Linear calibration curves (weighting 1/x ² ) were used for calculating the concentration in the plasma samples. Quality control samples for analytes were included. The deviation between nominal and calculated concentration in the calibrators and quality control samples were below 15% and the LLOQ sample was below 20%. PCSK9-LDL-R binding - Competitive (ELISA) This assay measures the apparent binding affinity to PCSK9 in competition with LDL-R. In particular the assay is used to evaluate the apparent binding affinity of an PCSK9 inhibitor such as an EGF(A) analogue and compounds comprising an EGF(A) analogue The assay is performed as follows. The day before the experiment, recombinant human Low Density Lipoprotein Receptor (rhLDL-R; NSO-derived; R & D systems # 2148-LD) is dissolved at 1 µg/ml in 50 mM sodium carbonate, pH 9.6, and then 100 µl of the solution is added to each well of the assay plates (Maxisorp 96, NUNC # 439454) and coated overnight at 4 °C. On the day of the experiments, 8 point concentration curves of the EGF(A) compounds containing Biotinylated PCSK9 (0.5 ug/ml, BioSite/BPSBioscience cat#71304) are made in duplicate. Test compound and biotinylated PCSK9 mixtures are prepared and incubated for 1 hour at room temperature in assay buffer containing 25 mM Hepes, pH 7.2 (15630-056, 100 ml, 1M), 150 mM NaCl (Emsure 1.06404.1000) 1 % HSA (Sigma A1887-25G) 0.05 % Tween 20 (Calbiochem 655205) 2 mM CaCl ₂ (Sigma 223506-500G). The coated assay plates are then washed 4x in 200 µl assay buffer, and then 100 µl of the mixture of test compounds and biotinylated PCSK9 is added to the plates and incubated 2 h at room temperature. The plates are washed 4x in 200 µl assay buffer and then incubated with Streptevadin-HRP (25ng/ml; VWR # 14-30-00) for 1 h at room temperature. The reaction is detected by adding 50 µl TMB-on (KEM-EN-TEC) and incubated 10 min in the dark. Then the reaction is stopped by adding 50 µl 4 M H ₃ PO ₄ to the mixture, added by electronic multi pipetting. The plates are then read in a Spectramax at 450 and 620 nm within 1 h. The 620 nm read is used for background subtraction. IC50 values are calculated using Graphpad Prism, by nonlinear regression log(inhibitor) vs. response-variable slope (four parameters), and converted into Ki values using the following formula: Ki=IC50/(1+(Biotin-PCSK9)/(kd(Biotin-PCSK9))), where Kd of the biotin-PCSK9 is 1.096727714 µg/ml and [Biotin-PCSK9] = 0.5 µg/ml. Higher Ki values reflects lower apparent binding affinities to PCSK9 and vice versa. A value above 500 nM, will indicate that the observed binding is not specific. Ki values for examples of EGF(A) peptide analogues and derivatives thereof are included below, showing that the high affinity of compounds having an EGF(A) peptide including 301L and optionally one or more of 309R, 312E and 321E is very similar also including compounds with one or two substituents attached to the N-terminal or a Lysine residue. EGF(A) peptide analogues Ki EGF(A) peptide derivatives, PCSK9i peptide therapeutics Example EGF(A) peptide SEQ ID NO Substituent Attachment Ki compound # site(s) (nM) 9 Example 1 - Preparation of compositions In order to evaluate the disintegration time for different solid composition comprising one or more absorption enhancer and optional a hydrotrope a series of tablets comprising SNAC, sodium caprate (NaC10), nicotinamide and magnesium stearate (MgSt) was prepared including the excipients as specified in the table 1.1 below. The tablets were prepared by initial granulation of the absorption enhancer(s) according to one or more of method 1 or 2 and 3, followed by the addition of extragranular MgSt in the final blending and compression as described by method 4 and 5 and indicated in table 1.1. Compositions T4-C1 and T4-D1 where prepared by separately granulating SNAC + nicotinamide by method 2 and NaC10 by method 3 followed by blending with magnesium stearate prior to compression, while compositions T4-C2 and T4-D2 were prepared by blending all ingredients prior to granulation by method 1. Tablets not including nicotinamide were punched in size 6,8x12 mm while the tablets including nicotinamide were punched in size 8x14 mm.

Table 1.1 – Tablet compositions expressed as mg per tablet. Example 2 – Disintegration of enhancer compositions The disintegration of the different tablet compositions of table 1.1 was evaluated using a small volume disintegration test (Assay I). Table 2.1 provides % disintegration after 25 and 30 minutes. It was surprisingly found that the disintegration of a tablet comprising SNAC, NaC10 and nicotinamide (T4 tablets) is accelerated compared to tablets including SNAC, SNAC and NaC10 or SNAC and nicotinamide (Ref -T1, -T2 and -T3 tablets). Table 2.1 Percent disintegration for the different compositions after 25 and 30 minutes. The results demonstrate that a tablet composition comprising SNAC, sodium caprate and nicotinamide disintegrate faster than any of the composition comprising only one or two of SNAC, sodium caprate and nicotinamide. Example 3 - Preparation of compositions comprising GLP-1 peptide compound and exposure of GLP-1 peptide after oral administration to beagle dogs Tablets with different amounts of different GLP-1 peptides, SNAC and further excipients were prepared. The content of the prepared compositions is provided in Tables 3.1 and 3.2. GLP-1 peptide 1 is Diacylated [Aib8,Arg34,Lys37]GLP-1(7-37) (Example 2 of WO2011/080103) GLP-1 peptide 2 is semaglutide which can be prepared as described in WO2011/080103. Semaglutide can be prepared according to the method described in WO2006/097537, Example 4 and SNAC can be prepared as described in WO2008/028859. A first series of tablet compositions comprising GLP-1 peptide 1 different ratios of SNAC/NA/NaC10 were prepared. The total amount of SNAC+NA+NaC10 was kept constant (= 167 mg) and the ratio of SNAC/NA maintained at 1.5, while the SNAC/NaC10 ratio was varied from 3.4 - 0.4 as set out in table 3.1 below. The tablet compositions were prepared by a combination of the methods 1-5 described above, whereby granules of SNAC + NA and NaC10 was obtained and subsequently mixed with magnesium stearate prior to compressions. Table 3.1 GLP-1 peptide 1 tablet compositions expressed as mg per tablet. A pharmacokinetic study was carried out to evaluate pharmacokinetic parameters after p.o. administration to Beagle dogs as described in assay II. Blood samples were drawn at predefined time points after dosing, and samples were analysed for concentration of the GLP-1 peptide. Based on these measurements plasma concentration versus time profile were plotted and a non-compartmental pharmacokinetic analysis of the data was performed. The plasma concentration of GLP-1 peptide measured over the first 30 minutes after dosing was used to evaluate the exposure observed for the different tablet compositions. The exposure following oral administration was evaluated as dose corrected exposure after 30 minutes (t=30 min /Cp/D_0.5hr), dose corrected AUC 0-30 min (AUC/D 0-0.5hr) and dose corrected maximum plasma concentration (Cmax/D) as set out in table 3.2. The table further includes the observed variability in plasma concentration of the GLP-1 peptide determined as %CV. The relative bioavailability is indicated by ++, +++, ++++, +++++, or ++++++, where ++++++ is used for the compositions providing the overall best results. Data for all compositions are obtained from dosing of 16 dogs, except Ref-T3 which was dose to 40 dogs. Table 3.2 Pharmacokinetic parameters obtained for the GLP-1 peptide 1 compositions of table 3.1. It was surprisingly found that the exposure of the GLP-1 peptide 1 was increased after administration of the compositions T4-F, T4-G, T4-H and, T4-I all comprising sodium caprate, whereof T4-G showed the highest exposure as illustrated in table 3.2. T4-G has almost equal amounts of SNAC and NaC10 and a bit less nicotinamide and thus the preferred ratio of SNAC : NaC10 : NA is around 100 : 67 : 100 (w:w:w). It is further observed that increasing the amount of NaC10 beyond 2.5 relative to SNAC is disadvantageous, and thus the preferred SNAC:NaC10 ratio is above 0.4. A second series of tablet compositions comprising GLP-1 peptide 2 was prepared to evaluate the exposure of GLP-1 peptide 2. The composition was prepared and tested as the GLP-1 peptide 1 tablet compositions. Table 3.3 GLP-1 peptide 2 tablet compositions. Tablet compositions expressed as mg per tablet. The disintegration of the different tablet compositions of table 3.3 was evaluated using a small volume disintegration test (Assay I). Table 3.4 provides % disintegration after 10 and 15 minutes.

Table 3.4 – Percent disintegration for the different compositions after 10 and 15 minutes. + indicates presence of excipient and (+) that the excipient is present but in a suboptimal amount. In agreement with the previous finding with GLP-1 peptide 1, a tablet comprising SNAC, NaC10 and nicotinamide (T4 tablets) disintegrates faster than tablets not including all three excipients (Ref -T1, -T2 and -T3 tablets). The compositions with the fastest disintegration were T4 – S6, T4 – S4 and T4 – G, whereof the two last mentioned tablet compositions differ only in terms of preparation methods A pharmacokinetic study was carried out with selected compositions to evaluate pharmacokinetic parameters after p.o. administration to Beagle dogs as described above and the results are included in table.3.5. Table 3.5 Pharmacokinetic parameters obtained for the GLP-1 peptide 2 compositions of table 3.3. Example 4 – Oral bioavailability in humans To further explore the ability of sodium caprate to increase the exposure of a GLP-1 peptide further compositions as set out in table 4.1. is prepared as described above. Table 4.1 GLP-1 peptide compound 2 tablet compositions. Tablet compositions expressed as mg per tablet. The oral bioavailability can further be explored in a pharmacokinetic study wherein subjects are administered p.o. a solid composition comprising a GLP-1 peptide. Blood samples are drawn at predefined time points after dosing, and samples analysed for concentration of the GLP-1 peptide. Based on these measurements plasma concentration versus time profile are plotted and a non-compartmental pharmacokinetic analysis of the data performed. Example 5 - Preparation of compositions comprising PCSK9 inhibitor and exposure of PCSK9 inhibitor after oral administration to beagle dogs Tablets with different amounts of PCSK9 inhibitor, SNAC and further excipients were prepared. The content of the prepared compositions is provided in Table 5.1 and 5.2. The PCSK9 inhibitor used is a peptide analogue of LDL-R293-332 comprising two substituents in the form of fatty diacids attached via a hydrophilic linker molecule. The EGF(A) derivative is prepared as described in WO2017/121850 (Example 151/page 161) and has the following structure and is described as compound H herein. The amino acid sequence is defined by SEQ ID No:16.: PCSK9i peptide tablets were prepared similar to as described in WO2021/023855 and WO2021/089761. In brief the tablet compositions included in table 5.1 were prepared by a combination of the methods 1-5 described above, whereby granules of SNAC + NA and NaC10 were separately obtained and subsequently mixed with API and magnesium stearate prior to compressions. The tablets compositions included in table 5.2 were prepared by physically blending SNAC and NA and separately granulating NaC10 by method 3 prior to mixing with API and magnesium stearate. The tablet compositions included in table 5.1 were prepared with the same SNAC/NA/NaC10 ratio but differing in weight. The tablet compositions in table 5.2 were prepared with different ratios of SNAC/NA/NaC10 while keeping the total amount of SNAC+NA+NaC10 constant (= 334 mg). The SNAC/NaC10 ratio was varied from about 12 to 0.1 and the SNAC/NA ration from about 20 to 0.1. Table 5.1 PCSK9 inhibitor tablet compositions. Tablet compositions expressed as mg per tablet. C T bl t PCSK9 SNAC N C10 Ni ti i M i T t l Table 5.2 PCSK9 inhibitor tablet compositions with different SNAC/NA/NaC10 ratios. Tablet compositions expressed as mg per tablet. A pharmacokinetic study was carried out to evaluate pharmacokinetic parameters after p.o. administration to Beagle dogs as described in Assay II above. Blood samples were drawn at predefined time points after dosing, and samples were analysed for concentration of the PCSK9 inhibitor. Based on these measurements plasma concentration versus time profile were plotted and a non-compartmental pharmacokinetic analysis of the data was performed. The plasma concentration of PCSK9 inhibitor measured over the first 30 minutes after dosing was used to evaluate the exposure observed for the different tablet compositions. The exposure following oral administration was evaluated as dose corrected exposure after 30 minutes (t=30 min /Cp/D_0.5hr), dose corrected AUC 0-30 min (AUC/D 0-0.5hr) and dose corrected maximum plasma concentration (Cmax/D) as set out in table 5.2. The relative bioavailability is indicated by ++, +++, ++++, +++++, or ++++++, where ++++++ is used for the compositions providing the overall best results. Data for all compositions are obtained from dosing of 16 dogs, except T4-F, where 32 dogs were dosed.

Table 5.4 Pharmacokinetic parameters obtained for the PCSK9 inhibitor compositions of table 5.1 and 5.2. It was surprisingly found that the exposure of the PCSK9 inhibitor was increased after administration of the compositions T4-E, T4-F, T4-G, T4-H, T4-S3 and T4- S5 all comprising SNAC, sodium caprate and nicotinamide, as compared to the reference compositions comprising only SNAC or SNAC/nicotinamide. Example 6 – Oral bioavailability of the PCSK9i peptide in humans To further explore the ability of sodium caprate to increase the exposure of a PCSK9i peptide further compositions as set out in table 6.1. is prepared as described above. Table 6.1 PCSK9i peptide tablet compositions. Tablet compositions expressed as mg per tablet. The oral bioavailability can further be explored in a pharmacokinetic study. Subjects are administered p.o. a solid composition comprising a GLP-1 peptide. Blood samples are drawn at predefined time points after dosing, and samples analysed for concentration of the GLP-1 peptide. Based on these measurements plasma concentration versus time profile are plotted and a non-compartmental pharmacokinetic analysis of the data performed. Example 7 - Preparation of compositions comprising a GLP-1 prodrug and exposure of GLP-1 prodrug after oral administration to beagle dogs Tablets with different amounts of a GLP-1 prodrug, SNAC and further excipients were prepared. The content of the prepared compositions is provided in Table 6.1. The GLP-1 prodrug is Gly-N ^α -2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethyl-Gly-semagluti de (SEQ ID No.: 26) with the structure The analogue and preparation thereof have previously been described in WO/2022/096636. The tablet compositions were prepared by a combination of the methods 1-5 described above, whereby granules of SNAC + NA and NaC10 were obtained and subsequently mixed with API and magnesium stearate prior to compressions. Composition Granulation GLP1 SNAC NaC10 Nicotinamide Magnesium Total Table 7.1 GLP-1 pro-drug tablet compositions. Tablet compositions expressed as mg per tablet. A pharmacokinetic study was carried out with T4 tablets in comparison with Ref – T2 and Ref – T3 tablets, to evaluate pharmacokinetic parameters after p.o. administration to Beagle dogs as described above and the results are included in table 7.2 below. Composition Cp/D 05hr AUC/D 0-05hr Cmax/D Relative Table 7.2 Pharmacokinetic parameters obtained for the GLP-1 prodrug compositions. For the GLP-1 prodrug the T4 tablet composition provided higher exposure compared to the reference tablet compositions T2 and T3 demonstrating an improvement by combining SNAC, sodium caprate and nicotinamide. By combining different enhances (SNAC and sodium caprate) and nicotinamide good exposure can be obtained with a smaller tablet which comprises less of SNAC, NaC10 and/or nicotinamide in total. Example 8 - Preparation of compositions comprising a GLP-1 GIP co-agonist and an insulin analogue and exposure after oral administration to beagle dogs Tablets comprising both a GLP-1 GIP co-agonist and an insulin analogue together with different amounts of SNAC and further excipients were prepared. The GLP-1 GIP co-agonist used is Y-Aib-EGTFTSDYSILLE-K[(2S)-2-amino-6-[[(2S)-2- amino-6-[[(4S)-4-carboxy-4-(17- carboxyheptadecanoylamino)butanoyl]amino]hexanoyl]amino]hexa noyl]- QAAREFIEWLLAGGPSSGAPPPS-OH (SEQ ID No.:25 with a substituent (HOOC-(CH ₂ ) ₁₆ -CO- gGlu-2xεLys-) attached via epsilon nitrogen of the lysine (K) in position 16). The insulin analogue used is A14E,B25H,B29K(N ^ε Octadecanedioyl- γGlu-OEG- OEG),desB30 human insulin (SEQ ID No.: 23 and 24 with a substituent ((HOOC-(CH ₂ ) ₁₆ -CO- γGlu-2xOEG-) attached via epsilon nitrogen of the Lysine (K) in position 29 of the B-chain (B29K) The tablet compositions were prepared by a combination of the methods 1-5 described herein above, whereby granules of SNAC + NA and NaC10 were obtained and subsequently mixed with API and magnesium stearate prior to compressions. The content and methods used to prepare the compositions are provided in Table 8.1. Composition Granulation GLP-1- Insulin SNAC NaC10 Nicotinamide Magnesium Total Table 8.1 GLP-1-GIP tablet compositions expressed as mg per tablet. A pharmacokinetic study was carried out with T4 tablet in comparison with Ref – T2 and Ref – T3, to evaluate pharmacokinetic parameters after p.o. administration to Beagle dogs as described above and the results are included in table 8.3 below. Composition Cp/D_0.5hr AUC/D 0-0.5hr Cmax/D Relative Table 8.2 - Pharmacokinetic parameters obtained for the GLP-1-GIP co-agonist of the compositions of table 8.1. Composition Cp/D_0.5hr AUC/D 0-0.5hr Cmax/D Relative Mean (kg/L) Mean (hr*kg/L) Mean (kg/L) bioavailability Table 7.4 - Pharmacokinetic parameters obtained for the insulin analogue of the compositions of table 8.1. For the GLP-1-GIP and Insulin compounds the T4 tablet composition provided higher exposure compared to the reference tablet compositions T2 and T3 demonstrating an improvement by combining SNAC, sodium caprate and nicotinamide. While certain features of the invention have been illustrated and described herein, many modifications, substitutions, changes, and equivalents will now occur to those of ordinary skill in the art. It is, therefore, to be understood that the appended claims are intended to cover all such modifications and changes as fall within the true spirit of the invention.