POLYPEPTIDE PROTRACTING TAGS FIELD OF THE INVENTION The present invention relates to compounds comprising a heterocyclic carboxylic acid bioisostere, methods for preparing the compounds and the medical applications of such compounds. BACKGROUND OF THE INVENTION It is often desirable to maintain well-defined concentrations of a given compound in the blood stream for a long time. This would for instance be the case when an immunogen is administered and a strong immune response is desired, or when a therapeutic target has to be exposed continuously to a therapeutic agent for a long time. Currently there are no universally applicable strategies to enhance the plasma half-life of any type of compound. The number of known endogenous polypeptides with interesting biological activities is growing rapidly, also as a result of the ongoing exploration of the human genome. Due to their biological activities, many of these polypeptides could in principle be used as therapeutic agents. Endogenous peptides are, however, not always suitable as drug candidates because these peptides often have half-lives of few minutes due to rapid degradation by peptidases and/or due to renal filtration and excretion in the urine. The half-life of polypeptides in human plasma varies strongly (from a few minutes to more than one week). Similarly, the half-life of small molecule drugs is also highly variable. The reason for this strong variability of plasma half-lives of peptides, proteins, or other compounds is, however, not well understood. Serum albumin has a half-life of more than one week, and one approach to increasing the plasma half-life of peptides has been to derivatised the peptides with a chemical entity that binds to serum albumin. Knudsen et al. (J. Med. Chem. 2000, 43,1664-1669) have shown that acylated GLP-1 peptides exhibit high receptor potency and a tenfold increase of plasma half-life in pigs. Zobel et al. (Bioorg. Med. Chem. Lett. 2003, 13, 1513-1515) have shown that the plasma half-life of an anticoagulant peptide in rabbits increased by 10-50 fold on derivatisation of the amino terminus with phosphate ester based small molecules binding to serum albumin. SUMMARY OF THE INVENTION According to the present invention there is provided a method for increasing the plasma half-life of a molecule, comprising covalently linking this molecule to a heterocyclic carboxylic acid bioisostere. The present invention also relates to a method for increasing the plasma half-life of a molecule, comprising covalently linking this molecule to a 1 H-tetrazole. According to the present invention there is also provided a method for increasing the plasma half-life of a molecule, comprising converting said molecule into a compound of the general formula (I): If V—G-X—Y-Z-A-Q- -R-molecule wherein G, X, and Y independently represent a bond, -S-, -O-, -NH-, -(CH2),.10-, or arylene, optionally substituted with one or more alkyl, amino, cycloalkyl, aryl, heteroaryl, halogen, nitro, lower alkoxy, hydroxy, MeCONH-, alkanoyl, or cyano, or heteroarylene, optionally substituted with one or more alkyl, amino, cycloalkyl, aryl, heteroaryl, halogen, nitro, lower alkoxy, hydroxy, MeCONH-, alkanoyl, or cyano, and Z represents a bond or -(CH:)n-, -0-(CH2)n-, -S-(CH2)n-, -(OCH2CH2)n-, -(CF2)n-, -O-CH2-(CF2)n-, -S-CH:-(CF2)n-, wherein n is 1-40, and A represents -C(=0)-, -O-C(=O)-, -NH-C(=O)-, -C(C=O)NH-S\=O)2-, -S(=O)2NH-C(=O)-, -O-(CH2)16-, or -0-(CH2),.5-C(=O)-, and Q represents a bond or -[NH-(CHsCH2OMCH2)p-E-C(=0)]q-tor -0-(CH2CH20)m-(CH2)p-E-C(=0)-,or -S-(CH2CH2O)m-(CH,)p-E-C(=0)-, wherein E is a bond, O, S, or NH, and m, p, and q independently are 1-40, and R represents a bond or a polyradical, such as [-NH(CH2)4CH(NH-)-C(=OH1.5, and t is 1-40, and the term 'molecule' refers to a compound comprising an amino group or a mercapto group, to which the group A or Q may be covalently linked. The present invention thus provides compounds of the general formula (I): -X—Y—Z-A-QtR-molecule (0 wherein G, X, and Y independently represent a bond, -S-, -O-, -NH-, -(CHj)^-, or arylene, optionally substituted with one or more alkyl, amino, cycloalkyl, aryl, r.eteroaryl, halogen, nitro, lower alkoxy, hydroxy, MeCONH-, alkanoyl, orcyano, or heteroarylene, optionally substituted with one or more alkyl, amino, cycloalky'., aryl, heteroaryl, halogen, nitro, lower alkoxy, hydroxy, MeCONH-, alkanoyl, or cyano, and Z represents a bond or -(CH2)n-, -CMCH,),,-, -S-(CH2)n-, -(OCH,CH2)n-, -(Cf,)n-, -O-CH?-(CF:)n-. -S-C-:-(CF2)n-, wherein n is 1-40. and A represents -C(O)-, -O-C(=O)-, -NH-C(O)-, -C(C=O)NH-S(=0)2-. -S(=O)jNH-C(=0)-, -(CHZ)14-, -O-(CH,), 5-, or -O-tCHzjLs-Ct^)-. and ! represents a bond or -[NH-(CH2CH20)m-(CH2)p-E-C(=0)]q-,or -0-(CH2CH20)m-(CH:)p-E-C(=0)-,or -S-(CH2CH2O)m-(CH:)p-E-C(=0)-, wherein E is a bond, 0, S, or NH, and m, p, and q independently are 1-40, and R represents a bond or a polyradical, such as [-NH(CH2)4CH(NH-)-C(=O)-]1.5, and tis 1-40, and the term 'molecule' refers to a compound comprising an amino group or a mercapto group, to which the group A or Q may be covalently linked. The present invention also provides a compound according to formula (I), wherein G, X and Y are all a bond. The present invention also provides a compound according to formula (I), wherein G, X and Y are all selected from -(CH2),.10-. The present invention aiso provides a compound according to formula (I), wherein t is 1. DEFINITIONS In the present specification, the following terms have the indicated meaning: The term "polyradical" means a molecule or molecular moiety with more than one unshared electron. A polyradical according to this definition may be used to covalently link two or more (mono-)radicals together. The term "small molecule drug" means a therapeutic agent with a molecular weight < 1500 g/moi. The term "therapeutic agent" means a peptide, protein, small molecule drug, or any other type of compound, able to elicit a biological response. The term "plasma half-life" means the time required for the concentration of a given compound present in the plasma of a living mammal, such as a human, to decrease to one half of its original concentration. The term "analog" refers to a polypeplide in which less than 30% of the amino acids of the original polypeptide have been removed or replaced by other amino acids (including stereoisomeric, unnatural or chemically modified amino acids) or have been chemically modified, for instance by acylation or alkylation of the side chain. The term "analog" also refers to poiypeptides in which the N-terminal amino group has been removed, alkylated with lower alkyl, or acylated with lower alkanoic, arylalkanoic, heteroarylalkanoic, or benzoic acids. The term "analog" also includes poiypeptides in which the C-terminal carboxyl group has been removed or converted to an amide by condensation with ammonia, lower aikyl amines, lower dialkyl amines, aziridine, azetidine, pyrroiidine, piperidine, orazepine. The term "analog" also includes poiypeptides in which the disulfide functionalities between two or more cystein groups have been reduced or the connectivity between two or more cystein groups has been modified. The term "derivative" as used herein in relation to a peptide means a.chemically modified peptide or an analogue thereof, wherein at least one substituent is not present in the unmodified peptide or an analogue thereof, i.e. a peptide which has been covalently modified. Typical modifications are amides, carbohydrates, alkyl groups, acyt groups, esters and the like. An example of a derivative of GLP-1(7-37) is Arg34Lys:f(Nt-(v-Glu(Na-hexadecanoyl)))-GLP- 1(7-37). The term "unnatural amino acid" refers to any compound comprising at least one primary or secondary amino group and at least one carboxyl group, without being L-alanine, L-arginine, L-asparagine, L-aspartic acid, L-cysteine, L-glutamine, L-glutamic acid, L-glycine, L-histidine, L-isoleucine, L-leucine, L-lysine, L-methionine, L-phenylalanine, praline, L-serine, L- threonine, L-tryptophan, L-tyrosine, orL-valine. The term "GLP-1(7-37)" refers to a peptide with the amino acid sequence HAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG (SEQ ID No. 1). The term "GLP-1 peptide" as used herein means GLP-1(7-37), a GLP-1 analog, a GLP-1 derivative or a derivative of a GLP-1 analog. In one embodiment the GLP-1 peptide is an insulinotropic agent. The term "exendin-4(1-39)" refers to a peptide with the arnino acid sequence HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS (SEQ ID No. 2). The term "insulinotropic agent" as used herein means a compound which is an agonist of the human GLP-1 receptor, i.e. a compound which stimulates the formation of cAMP in a suitable medium containing the human GLP-1 receptor. The potency of an insulinotropic agent is determined by calculating the EC50 value from the dose-response curve as described below. Baby hamster kidney (BHK) cells expressing the cloned human GLP-1 receptor (BHK-467-12A) were grown in DMEM media with the addition of 100 ILJ/mL penicillin, 100/yL/mL streptomycin, 10% fetal calf serum and 1 mg/mL Geneticin G-418 (Life Technologies). Plasma membranes were prepared by homogenisation in buffer (10 mM Tris-HCI, 30 mM NaCI and 1 mM dithiothreitol, pH 7.4, containing, in addition, 5 mg/L leupeptin (Sigma, St. Louis, MO, USA), 5 mg/L pepstatin (Sigma), 100 mg/L bacitracin (Sigma), and 16 mg/L aprotinin (Calbiochem-Novabiochem, La Jolla, CA). The homogenate was centrifuged on top of a layer of 41 w/v% sucrose. The white band between the two layers was diluted in buffer and centrifuged. Plasma membranes were stored at -80°C until used. The functional receptor assay was carried out by measuring cAMP as a response to stimulation by the insulinotropic agent. Incubation were carried out in 96-well microtiter plates in a total volume of 140 //L and with the following final concentrations: 50 mM Tris-HCI, 1 mM EGTA, 1.5 mM MgSO,, 1.7 mM ATP, 20 mM GTP, 2 mM 3-isobutyl-1-methylxanthine (IBMX), 0.01 % Tween-20, pH 7.4. Compounds to be tested for agonist activity were dissolved and diluted in buffer. GTP was freshly prepared for each experiment: 2.5 fjg of membrane was added to each well and the mixture was incubated for 90 min at room temperature in the dark with shaking. The reaction was stopped by the addition of 25 /^L of 0.5 M HCI. Formed cAMP was measured by a scintillation proximity assay (RPA 542, Amersham, UK). Dose-response curves were plotted for the individual compounds and EC50 values calculated using GraphPad Prism software. The term "DPP-IV protected" as used herein referring to a polypeptide means a polypeptide which has been chemically modified in order to render said compound resistant to the plasma peptidase dipeptidyl aminopeptidase-4 (DPP-IV). The DPP-IV enzyme in plasma is known to be involved in the degradation of several peptide hormones, e.g. GLP-1, GLP-2, Exendin-4 etc. Thus, a considerable effort is being made to develop analogues and derivatives of the polypeptides susceptible to DPP-IV mediated hydrolysis in order to reduce the rate of degradation by DPP-IV. Resistance of a peptide to degradation by dipeptidyl aminopeptidase IV is determined by the following degradation assay : Aiiquots of the peptide (5 nmol) are incubated at 37 °C with 1 /;L of purified dipeptidyl aminopeptidase IV corresponding to an enzymatic activity of 5 ml) for 10-180 minutes in 100 fjl of 0.1 M triethylamine-HCI buffer, pH 7.4. Enzymatic reactions are terminated by the addition of 5 /jl of 10% trifluoroacetic acid, and the peptide degradation products are separated and quantified using HPLC analysis. One method for performing this analysis is : The mixtures are applied onto a Vydac C18 widepore (30 nm pores, 5//m particles) 250 x 4.6 mm column and eluted at a flow rate of 1 ml/min with linear stepwise gradients of acetonitrile in 0.1% trifluoroacetic acid (0% acetonitrile for 3 min, 0-24% acetonitrile for 17 min, 24-48% acetonitrile for 1 min) according to Siegel et al., Regul. Pept. 1999;79:93-102 and Mentlein et al. Eur. J. Biochem. 1993;214:829-35. Peptides and their degradation products may be monitored by their absorbance at 220 nm (peptide bonds) or 280 nm (aromatic amino acids), and are quantified by integration of their peak areas related to those of standards. The rate of hydrolysis of a peptide by dipeptidyl aminopeptidase IV is estimated at incubation times which result in less than 10% of the peptide being hydrolysed. The term "factor VII" refers to the human factor VII of the blood clotting cascade. The term "bioisostere" refers to a molecular fragment capable of mimicking the biological properties of another mo;ecular fragment. Typical bioisosteres of carboxylic acids include tetrazoles, phenols, N-acylsulfonamides, or other compounds with an acidic NH- or OH-group. The term "halogen" means F, Cl, Br or I. The term "alky!" as used nerein is intended to mean straight, branched, or cyclic C,-C-0 alkyl. The term "lower alkyl" refers to C,-C6 alkyl. The term "aryl" as used herein is intended to include carbocyclic aromatic ring systems such as phenyl, biphenylyl, naphthyl, anthracenyl, phenanthrenyl, fluorenyl, indenyl, pentalenyl, azulenyl and the like. Ar\! is also intended to include the partially hydrogenated derivatives of the carbocyclic systems enumerated above. Non-limiting examples of such partially hydrogenated derivatives are 1,2,3,4-tetrahydronaphthyl, 1,4-dihydronaphthyl and the like. The term "arylene" as used herein is intended to include arene-derived diradicals such as 1,2-phenylene, 1,3-phenylene, 1,4-phenylene, 1,2-naphthylene, 1,4-naphthylene, 4,4'-biphenylene, 4,4"-terphenylene, 4,4'"-quaterphenylene, and the like. The term "heteroarylene as used herein is intended to include heteroarene-derived diradicals, such as 1,2,4-pyrazol-2,5-diyl, imidazol-1,2-diyl, thiazol-2,4-diyl, and the like, as well as combinations of arylene with heteroarylene diradicals, such as (4-phenylimidazote)-4,1'-diyl, (3,5-diphenyl-1,2,4-oxadiazole)-4,4"-diyl, and the like. The term "aryloxy" as used herein refers to the radical -O-aryl where aryl is as defined above. Non-limiting examples are phenoxy, naphthoxy, anthracenyloxy, phenanthrenyloxy, fluorenyloxy, indenyloxy and the like. The term "heteroaryl" as used herein is intended to include heterocyclic aromatic ring systems containing one or more heteroatoms selected from nitrogen, oxygen and sulfur such as furyl, thienyl, pyrrolyl, oxazolyl, thiazolyl, imidazolyl, isoxazolyl, isothiazolyl, 1,2,3-triazolyl, 1,2,4-triazolyl, pyranyl, pyridyl, pyridazinyl, pyrimidinyl, pyrazinyl, 1,2,3-triazinyl, 1,2,4-triazinyl, 1,3,5-triazinyl, 1,2,3-oxadiazolyl, 1,2.4-oxadiazolyl, 1,2,5-oxadiazolyl. 1,3,4-oxadiazolyl, 1,2,3-thiadiazolyl, 1,2,4-thiadiazolyl, 1,2,5-thiadiazolyl, 1,3,4-thiac.azolyl, tetrazolyl, thiadiazinyl, indolyl, isoindolyl, benzofuryl, benzothienyl, indazolyl, benzimidazolyl, benzthiazolyl, benzisothiazolyl, benzoxazolyl, benzisoxazolyl, purinyl, quinazoiinyl, quinolizinyl, quinolinyl, isoquinolinyl, quinoxalinyl, naphthyridinyl. pteridinyl, carbazolyl, azepinyl, diazepinyl, acridinyl and the like. Heteroaryl is also intended to include the partially hydrogenated derivatives of the heterocyclic systems enumerated above. Non-limiting examples of such partially hydrogenated derivatives are 2,3-dihydrobenzofuranyl, pyrrolinyl, pyrazolinyl, indanyl, indolinyl, oxazolidinyl, oxazolinyl, oxazepinyl and the like. Certain of the above defined terms may occur more than once in the structural formulae, and upon such occurrence each term shall be defined independently of the other. The term "optionally substituted" as used herein means that the groups in question are either unsubstituted or substituted with one or more of the substituents specified. Wnen the groups in question are substituted with more than one substituent the substituents may be the same or different. DETAILED DESCRIPTION OF THE INVENTION In one aspect the present invention provides a method for increasing the plasma half-life of a molecule, comprising covalently linking this molecule to a heterocyclic carboxylic acid bioisostere. In another aspect the present invention provides a method for increasing the plasma half-life of a molecule, comprising covalently linking this molecule to a 1H-tetrazole. In In another aspect the present invention provides a method for increasing the plasma half-life of a molecule, comprising converting said molecule into a compound of the general formula 0): H -*{ (1) wherein G, X, and Y independently represent a bond, -S-, -C-. -NH-, -(CH:)...-. or arylene, optionally substituted with one or more alkyl, amino, cycloalkyl, aryl, heteroaryl, halogen, nitro, lo\-.er alkoxy, hydroxy, MeCONH-, alkanoyl, orcyano, or heteroarylene, optionally substituted with one or more alky!, amino, cycloalkyl, aryl, heteroaryl, halogen nitre, lower alkoxy. hydroxy, MeCONH-, alkanoyl, orcyano,.and Z represents a bc~d or -(CH,)n-, -0-, CH,.}.,-. -S-(CH-).-, -(OCH2CH2)n-, -(CF2)n-, -O-CH2-(CF2)n-, -S-CHr. wherein if V-G-X-Y-Z-A-Q H is 16-(5~tetrazolyl)h exadecanoyl, 4-[N-(16-{5-tetrazo . l}hexadecanoyl)suifamoyl]butyryl, 2-(2-(2-(16-(tetrazc -5-yl)(hexadecanoylamino)ethoxy)ethoxy)acetyl) or 16-(1H-tetrazol-5-> ihexadecanoic acid [2-(2-{[2-(2-carbamoylmethox>ethoxy)ethylcarbamoyl]methoxy}ethoxy)ethyl]amide. In another embodiment the invention provides a compound according to formula ), wherein the molecule is co. aiently linked to R via the t-amino group of a lysine residue. In another embodiment the invention provides a compound according to formula I), wherein the molecule is cc% aiently linked to R via the thiol group of a cysteine residue. In another embodiment the invention provides a compound according to formula (I), wherein the molecule is a therapeutic agent. in another aspect the invention provides a compound according to formula (I), wherein the therapeutic agent is a biopolymer. In another aspect the invention provides a compound according to formula (I), wherein the therapeutic agent is a polypeptide. In another aspect the invention provides a compound according to formula (I), wherein the therapeutic agent is a small molecule drug. In another aspect the present invention provides a compound according tofoimula (I), wherein the molecule is a polypeptide which is an insulinotropic peptide. In one embodiment the invention provides a compound according to formula (I), wherein the molecule is a polypeptide which is GLP-1(7-37) or a variant thereof. In another embodiment the invention provides a compound according to formula (I), wherein the molecule is a polypeptide which is GLP-1(7-37) or an analog thereof. In another embodiment the invention provides a compound according to formula (I), wherein the molecule is a polypeptide comprising the amino acid sequence of the formula (IV): XaarXaa8-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Xaa16-Ser-Xaa1B-Xaa19-Xaa2o-Glu-Xaa22-Xaa:3-Ala- Formula (III) (SEQ ID No: 3) wherein Xaa is L-histidine, D-histidine, desamino-histidine, 2-amino-3-(2-aminoimidazol-4-yl)propionic acid, (3-hydroxy-histidine, homohistidine, N"-acetyl-histidine, a-fluoromethyl-histidine, a-methyl-histidine, 3-pyridylalanine, 2-pyridylalanine or4-pyridylalanine; Xaaa is Ala, Gly, Val, Leu, lie, Lys, Aib, 1-aminocyclopropanecarboxylic acid, 1-aminocyclobutanecarboxylic acid, 1 -aminocyclopentanecarboxylic acid, 1- aminocyclohexanecarboxylic acid, 1-aminocycloheptanecarboxylic acid, or 1- aminocyclooctanecarboxylic acid; Xaa,s is Val or Leu; Xaa1g is Ser, Lys or Arg; Xaa19 is Tyror Gin; Xaa20 is Leu or Met; Xaa22 is Gly, Glu or Aib; Xaa23 is Gin, Glu, Lys or Arg; Xaa2S is Ala or Val; Xaa26 is Lys, Glu or Arg; Xaa27 is Glu or Leu; Xaa30 is Ala, Glu or Arg; Xaa33 is Val or Lys; Xaa34 is Lys, Glu, Asn or Arg; Xaa35 is Gly or Aib; Xaa36 is Arg, Gly or Lys; Xaa37 is Gly, Ala, Glu, Pro, Lys, amide or is absent; Xaa3a is Lys, Ser, amide or is absent; Xaa39 is Ser, Lys, amide or is absent; Xaa40 is Gly, amide or is absent; Xaa41 is Ala, amide or is absent; Xaa42 is Pro, amide or is absent; Xaa43 is Pro, amide or is absent; Xaa44 is Pro, amide or is absent; Xaa45 is Ser, amide or is absent; Xaa46 is amide or is absent; provided that if Xaa36, Xaa39, Xaa40, Xaa41, Xaa42, Xaa43, Xaa44, Xaa45 or Xaa46 is absent then each amino acid residue downstream is also absent. in another embodiment the invention provides a compound according to formula (I), wherein the molecule is a polypeptide comprising the amino acid sequence of formula (V): XaarXaa8-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-Xaa18-Tyr-Leu-Glu-Xaa22-Xaa23-Ala-Ala-Xaa26-Glu-Phe-lle-Xaa30-Trp-Leu-Val-Xaa34-Xaa35-Xaa36-Xaa37-Xaa38 Formula (IV) (SEQ ID No: 4) wherein Xaa7 is L-histidine, D-histidine, desamino-histidine, 2-aminohistidine, p-hydroxy-histidine, homohistidine, N°-acetyl-histidine, a-fluoromethyl-histidine, a-methyl-histidine, 3- pyridylalanine, 2-pyridylalanine or 4-pyridylalanine; Xaa8 is Ala, Gly, Val, Leu, lie, Lys, Aib, 1-aminocyclopropanecarboxylic acid, 1- aminocyclobutanecarboxylic acid, 1-aminocyclopentanecarboxylic acid, 1- aminocyclohexanecarboxylic acid, 1-aminocycloheptanecarboxylic acid, or 1- aminocyclooctanecarboxylic acid; Xaa18 is Ser, Lys or Arg; Xaa22 is Gly, Glu or Aib; Xaa23 is Gin, Glu, Lys or Arg; Xaa26 is Lys, Glu or Arg; Xaa30 is Ala, Glu or Arg; Xaa34 is Lys, Glu or Arg; Xaa35 is Gly or Aib; Xaa36 is Arg or Lys;' Xaa37 is Gly, Ala. Glu or Lys; Xaa38 is Lys, amide or is absent. In another embodiment the invention provides a compound according to formula (I1!, wherein the molecule is a polypeptide selected from GLP-1(7-35), GLP-1(7-36), GLP-1(7-36!-amide, GLP-1(7-37), GLP-1(7-38), GLP-1(7-39), GLP-1(7-40), GLP-1(7-41) or an analog thereof. In another embodiment the invention provides a compound according to formula (I), wherein the molecule is a polypeptide comprising no more than fifteen amino acid residues which have been exchanged, added or deleted as compared to GLP-1(7-37) (SEQ ID No. 1), or no more than ten amino acid residues which have been exchanged, added or deleted as compared to GLP-1(7-37) (SEQ ID No. 1). In another embodiment the invention provides a compound according to formula (I;. wherein the molecule is a polypeptide comprising no more than six amino acid residues which have been exchanged, added or deleted as compared to GLP-1(7-37) (SEQ ID No. 1). in another embodiment the invention provides a compound according to formula (I), wherein the molecule is a polypeptide comprising no more than 4 amino acid residues which are not encoded by the genetic code. In another embodiment the invention provides a compound according to formula (I), wherein the molecule is a polypeptide which is a DPP-IV protected insulinotropic peptide. In another embodiment the invention provides a compound according to formula (I), wherein the molecule is a polypeptide comprising an Aib residue in position 8. In another embodiment the invention provides a compound according to formula (I), wherein the molecule is a GLP-1(7-37) analog wherein the amino acid residue in position 7 of said polypeptide is selected from the group consisting of D-histidine, desamino-histidine, 2-amino-3-(2-aminoimidazol-4-yl)propionic acid, p-hydroxy-histidine, homohistidine, N"-acetyl-histidine, a-fluoromethyl-histidine, a-methyl-histidine, 3-pyridylalanine, 2-pyridylalanine and 4-pyridylalanine. In another embodiment the invention provides a compound according to formula (I), wherein the molecule is a GLP-1(7-37) analog selected from the group consisting of Arg34GLP-1(7- 37), Lys38Arg26'34GLP-1(-7-38), Lys38Arg26'34GLP-1(7-38)-OH, Lys36Arg26'34GLP-1(7-36), Aib8-2r:3f'GLP-1 (7-37), Aib6'36GLP-1 (7-37), Aib8'22 GLP-1 (7-37), Aib8•22'35 Arg:634Lys:'6GLP-1 (7-38), Aib8'35 Arg26-34Lys38GLP-1 (7-38), Aib8'22 Arg:s34Lys38GLP-1 (7-38), Aib8'22'35 Arg26'34Lys38GLP-1 (7-38), Aib8 35 Arg:634LysMGLP-1 (7-38), Aib8'22'35 Arg26Lys3pGLP-1 (7-38), Aib8-35 Arg:6Lys38GLP-1 (7-38), Aib"2 Arg26Lys38GLP-1 (7-38), Aib8'22 35Arg34Lys38GLP-1 (7-38), Aib3'35Arg3Yys3SGLP-1 (7-38), Aib8'22Arg34Lys3SGLP-1 (7-38), Aib8'22::5AlairLys38GLP-1 (7-38), Aib8'35Ala37Lys38GLP-1 (7-38), Aiba'22Ala37Lys38GLP-1 (7-38), Aib822 "Lys37GLP-1 (7-37), Aibe'35Lys37GLP-1(7-37) and Aib8'22Lys37GLP-1(7-38). In another embodiment the invention provides a compound according to formula (I), wherein the molecule is GLP-1 (7-37) or an analog thereof which is attached to R via the amino acid residue in position 23, 26, 34, 36 or 38 relative to the amino acid sequence SEQ ID No:1. In another aspect the present invention provides a compound according to formula (I), wherein the molecule is exendin-4(1-39) or an analog thereof. In one embodiment the invention provides a compound according to formula (I), wherein the molecule is an exendin-4 analog comprising no more than twelve amino acid residues which have been exchanged, added or deleted as compared to exendin-4(1-39) (SEQ ID No. 2), or no more than eight amino acid residues which have been exchanged, added or deleted as compared to exendin-4(1-39) (SEQ ID No. 2). In another embodiment the invention provides a compound according to formula (I), wherein the molecule is ZP-10, i.e. HGEGTFTSDLSKQMEEEAVRLFiEWLKNGGPSSGAPPSKKKKKK-amide (SEC ID No. 5). In another embodiment the invention provides a compound according to formula (I), wherein said compound is selected from tne group consisting of NH--26-(16-[5-tetrazolyl]hexadecanoyl)ArgLUGLP-1-(7-37), Gly8,Arg26'MGLP-1(7-37)Lys(16-(5-tetrazolyl)hexadecanoyl), Gly6,Arg:634GLP-1i7-37)Lys{4-[N-(16-{5-tetrazolyl}hexadecanoy!)sulfamoyl]butyryl}, N-e-26-{4-[N-(16-{5-tetrazolyl}hexadecanoyl)sulfamoy!]butyryl) Arg34GLP-1(7-37), N-£-37-(2-(2-(2~(16-(tetrazol-5-ylj(hexadecanoylamino)ethoxy)ethoxy)acetyl)) Aib822'36Lys37GLP-1(7-37), Gly8,Glu22'23'30Arg1s';65~GLP-1(7-37)Lys(16-(1H-tetrazol-5-yl)hexadecanoicacid ;2-(2-{[2-(2-carbamoylmethoxyethoxy)ethylcarbamoyl]methoxy}ethoxy)ethyl]amide)-NH2, ard Gly8Arg2634GLP-1(7-37)Lys(4-(4-«:4-(4-(5-tetrazolyl)phenyl)phenyl)phenoxy)buh"yl).N-e38-(2-(2-(2-(16-(4-(5-letrazolyl)phenox/)hexadecanoyl)ethoxy)ethoxy)acetyl) [GlyO,Arg26,34,Lys38]GLP-1 (7-37) peptide N-epsilon37-(2-(2-(2-( 16-(4-(5-Tetrazolyl)phenoxy)hexadecanoyl)ethoxy)ethoxy)acetyl)[Aib8,22,35.Lys37]GL?-1 (7-37) Nc37-(16-(4,5-Bis(5-Tetrazolyl)imidazol-1-yl)hexadecanoyl)[Gly8,Arg26,34]GLP-1-(7-37) peptide Nt37-((2-(2-(16-i5-Tetrazolyl)hexadecanoylamino) ethoxy)ethoxy «acetyl)[Gly8,Arg26,34]GLP-1 -(7-37) peptide Nt26-(4-{16-(Tetrazol-5-yl)hexadecanoylsulfamoyl}butyryl)[(3-(4-imidazolyl)propionyl7,Arg34]GLP-1-(7-37) peptide I .'. '.'i I \l R G K G-COOH NE;M-(16-{Tetra2ol-5-yl}hexadecanoyl)-[Gly8. Arg26] GLP-1 (7-34) pepticeamide T S !) V S S Y L E G Q A A R I A W L V-N H Nt2*-({2-[2-(4-(16-(Tetrazol-5-yl)hexadecanoylsutfamoyl)butyrylamino)ethoxy]ethoxy}acetyl)-[Arg34] GLP-1 (7-37) peptide N£S<-({2-[2-(4-(16-(Tetrazol-5-yl)hexadecanoylsulfamoyl)butyrylamino)ethoxy]ethoxy}acetyl)-[Arg26] GLP-1 (7-34) peptideamide N -({2-[2-(4-(16-(Tetrazol-5- yl)hexadecanoylsulfamoyl)butyrylamino)ethoxy]ethoxy}acetyl)-[(3-(4-imidazolyl)propionyl)7,Arg34]GLP-1 (7-37) peptide N'':ns thereof can be used. The amount to be added should be an amount sufficient to inhibit c • dation of the methionine residues such that the amount of methionine sulfoxide is acceptazie to regulatory agencies. Typically, this means that the composition contains no more :nan about 10% to about 30% methionine sulfoxide. Generally, this can be achieved by adc -3 methionine such that the ratio of methionine added to methionine residues ranges from about 1:1 to about 1000:1, such as 10:1 to about 100:1. In a further embodiment of the invention the formulation furthe* comprises a stabiliser selected from the group of high molecular weight polymers or low m: ecular compounds. In a further embodiment of the invention the stabilizer is selected fr; TI polyethylene glycol (e.g. PEG 3350), polyvinylalcohol (PVA), polyvinylpyrrolidore carboxy-/hydroxycellulose or derivates thereof (e.g. HPC, HPC-SL, HPC-L and HPMC). cyclodextrins, sulphur-containing substances as monothioglycerol, thioglycolic a: d and 2-methylthioethanol, and different salts (e.g. sodium chloride). Each one of these specific stabilizers constitutes an alternative embodiment of the invention. The pharmaceutical compositions may also comprise addition?, stabilizing agents, which further enhance stability of a therapeutically active polypeptide tre-ein. Stabilizing agents of particular interest to the present invention include, but are - ot limited to, methionine and EDTA, which protect the polypeptide against methionine oxidat rn, and a nonionic surfactant, which protects the polypeptide against aggregation associa:ed with freeze-thawing or mechanical shearing. In a further embodiment of the invention the formulation furthe- comprises a surfactant. In a further embodiment of the invention the surfactant is selectee ~rom a detergent, ethoxylated castor oil, polyglycolyzed glycerides, acetylated monogi.. oerides, sorbitan fatty acid esters, polyoxypropylene-polyoxyethylene block polymers (eg. poloxamers such as Plutonic* F68, poloxamer 188 and 407, Triton X-100 ), polyoxyethylene sorbitan fatty acid esters, polyoxyethylene and polyethylene derivatives such as alkylated and alkoxylated derivatives (tweens, e.g. Tween-20, Tween-40, Tween-80 and Brij-35), monoglycerides or ethoxylated derivatives thereof, diglycerides or polyoxyethylene derivatives thereof, alcohols, glycerol, lecitins and phospholipids (eg. phosphatidyl serine, phosphatidyl choline, phosphatidyl ethanolamine, phosphatidyl inositol, diphosphatidyl glycerol and sphingomyelin), derivates of phospholipids (eg. dipalmitoyl phosphatidic acid) and lysophospholipids (eg. palmitoyl lysophosphatidyl-L-serine and 1-acyl-sn-glycero-3-phosphate esters of ethanolamine, choline, serine orthreonine) and alkyl, alkoxyl (alkyl ester), alkoxy (alkyl ether)- derivatives of lysophosphatidyl and phosphatidylcholines, e.g. lauroyl and myristoyl derivatives of lysophosphatidylcholine, dipaimitoylphosphatidylcholine, and modifications of the polar head group, that is cholines, ethanolamines. phosphatidic acid, serines, threonines, glycerol, inositol, and the positively charged DODAC, DOTMA, DCP, BISHOP, lysophosphatidylserine and lysophosphatidylthreonine, and glycerophospholipids.(eg. cephalins), glyceroglycolipids (eg. galactopyransoide), sphingoglycolipids (eg. ceramides, gangliosides), dodecylphosphocholine, hen egg lysolecithin, fusidic acid derivatives- (e.g. sodium tauro-dihydrofusidate etc.), long-chain fatty acids and salts thereof C6-C12 (eg. oleic acid and caprylic acid), acylcarnitines and derivatives, N"-acylated derivatives of lysine, arginine or histidine, or side-chain acylated derivatives of lysine or arginine, N"-acylated derivatives of dipeptides comprising any combination of lysine. arginine or histidine and a neutral or acidic amino acid, Na-acylated derivative of a tripeptide comprising any combination of a neutral amino acid and two charged amino acids. DSS (docusate sodium, CAS registry no [577-11-7]). docusate calcium, CAS registry no [128-49-4]), docusate potassium, CAS registry no [7491-09-0]), SDS (sodium dodecyi sulfate or sodium lauryl sulfate), sodium caprylate. cholic acid or derivatives thereof, bile acids and salts thereof and glycine ortaurine conjugates, ursodeoxycholic acid, sodium cholate, sodium deoxycholate, sodium taurocholate, sodium glycocholate. N-hexadecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate, anionic (alkyl-aryl-sulphonates) monovalent surfactants, zwitterionic surfactants (e.g. N-alkyi-N,N-dimethylammonio-1-propanesulfonates, 3-cholamido-1-propyldimethylammonio-1-propanesulfonate, cationic surfactants (quarternary ammonium bases) (e.g. cetyl-trimethylammonium bromide, cetylpyridinium chloride), non-ionic surfactants (eg. dodecyi f>-D-glucopyranoside), poloxamines (eg. Tetronic's), which are tetrafunctional block copolymers derived from sequential addition of propylene oxide and ethylene oxide to ethylenediamine, or the surfactant may be selected from the group of imidazoline derivatives, or mixtures thereof. Each one of these specific surfactants constitutes an alternative embodiment of the invention. The use of a surfactant in pharmaceutical compositions is well-known to the skilled person. For convenience reference is made to Remington: The Science and Practice of Pharmacy, 19th edition, 1995. It is possible that other ingredients may be present in the peptide pharmaceutical formulation of the present invention. Such additional ingredients may include wetting agents, emulsifiers, antioxidants, bulking agents, tonicity modifiers, chelating agents, metal ions, oleaginous vehicles, proteins (e.g., human serum albumin, gelatin or proteins) and a zwitterion (e.g., an amino acid such as betaine, taurine, arginine, glycine, lysine and histidine). Such additional ingredients, of course, should not adversely affect the overall stability of the pharmaceutical formulation of the present invention. Pharmaceutical compositions containing a compound according to the present invention may be administered to a patient in need of such treatment at several sites, for example, at topical sites, for example, skin and mucosal sites, at sites which bypass absorption, for example, administration in an artery, in a vein, in the heart, and at sites which involve absorption, for example, administration in the skin, under the skin, in a muscle or in the abdomen. Administration of pharmaceutical compositions according to the invention may be through several routes of administration, for example, lingual, sublingual, buccal. in the mouth, oral, in the stomach and intestine, nasal, pulmonary, for example, through the bronchioles and alveoli or a combination thereof, epidermal, dermal, transdermai. vaginal, rectal, ocular, for examples through the conjunctiva, uretal, and parenteral to patients in need of such a treatment. Compositions of the current invention may be administered in several dosage forms, for example, as solutions, suspensions, emulsions, microemulsions, multiple emulsion, foams, salves, pastes, plasters, ointments, tablets, coated tablets, rinses, capsules, for example, hard gelatine capsules and soft gelatine capsules, suppositories, rectal capsules, drops, gels, sprays, powder, aerosols, inhalants, eye drops, ophthalmic ointments, ophthalmic rinses, vaginal pessaries, vaginal rings, vaginal ointments, injection solution, in situ transforming solutions, for example in situ gelling, in situ setting, in situ precipitating, in situ crystallization, infusion solution, and implants. Compositions of the invention may further be compounded in, or attached to, for example through covalent, hydrophobic and electrostatic interactions, a drug carrier, drug delivery system and advanced drug delivery system in order to further enhance stability of the compound, increase bioavailability, increase solubility, decrease adverse effects, achieve chronotherapy well known to those skilled in the art, and increase patient compliance or any combination thereof. Examples of carriers, drug delivery systems and advanced drug delivery systems include, but are not limited to, polymers, for example cellulose and derivatives, polysaccharides, for example dextran and derivatives, starch and derivatives, poly(vinyl alcohol), acrylate and methacrylate polymers, polylactic and polyglycolic acid and block co-polymers thereof, polyethylene glycols, carrier proteins, for example albumin, gels, for example, thermogelling systems, for example block co-polymeric systems well known to those skilled in the art, micelles, liposomes, microspheres, nanoparticulates, liquid crystals and dispersions thereof, L2 phase and dispersions there of, well known to those skilled in the art of phase behaviour in lipid-water systems, polymeric micelles, multiple emulsions, self-emulsifying, self-microemulsifying, cyclodextrins and derivatives thereof, and dendrimers. Compositions of the current invention are useful in the formulation of solids, semisolids, powder and solutions for pulmonary administration of the compound, using, for example a metered dose inhaler, dry powder inhaler and a nebulizer, all being devices well known to those skilled in the art. Compositions of the current invention are specifically useful in the formulation of controlled, sustained, protracting, retarded, and slow release drug delivery systems. More specifically, but not limited to, compositions are useful in formulation of parenteral controlled release and sustained release systems (both systems leading to a many-fold reduction in number of administrations), well known to those skilled in the art. Even more preferably, are controlled release and sustained release systems administered subcutaneous. Without limiting the scope of the invention, examples of useful controlled release system and compositions are hydrogels, oleaginous gels, liquid crystals, polymeric micelles, microspheres, nanoparticles, Methods to produce controlled release systems useful for compositions of the current invention include, but are not limited to, crystallization, condensation, co-cystallization, precipitation, co-precipitation, emulsification, dispersion, high pressure homogenization, encapsulation, spray drying, microencapsulation, coacervation, phase separation, solvent evaporation to produce microspheres, extrusion and supercritical fluid processes. General reference is made to Handbook of Pharmaceutical Controlled Release (Wise, D.L., ed. Marcel Dekker, New York, 2000) and Drug and the Pharmaceutical Sciences vol. 99: Protein Formulation and Delivery (MacNally, E.J., ed. Marcel Dekker, New York, 2000). Parenteral administration may be performed by subcutaneous, intramuscular, intraperitoneal or intravenous injection by means of a syringe, optionally a pen-like syringe. Alternatively, parenteral administration can be performed by means of an infusion pump. A further option is a composition which may be a solution or suspension for the administration of the compound according to the present invention in the form of a nasal or pulmonal spray. As a still further option, the pharmaceutical compositions containing the compound of the invention can also De adapted to transdermal administration, e.g. by needle-free injection or from a patch, optionally an iontophoretic patch, or transmucosal, e.g. buccal, administration. The term "stabilized formulation" refers to a formulation with increased physical stability, increased chemical stability or increased physical and chemical stability. The term "physical stability" of the protein formulation as used herein refers to the tendency of tre protein to form biologically inactive and/or insoluble aggregates of the protein as a result c* exposure of the protein to thermo-mechanical stresses and/or interaction with inte~"aces and surfaces that are destabilizing, such as hydrophobic surfaces and interfaces. Ph>; ;cal stability of the aqueous protein formulations is evaluated by means of visual inspection and/or turbidity measurements after exposing the formulation filled in suitable containers e.g. cartridges or vials) to mechanical/physical stress (e.g. agitation) at different temperatures for various time periods. Visual inspection of the formulations is performed in a shaT> focused light with a dark background. The turbidity of the formulation is characterized by a visual score ranking the degree of turbidity for instance on a scale from 0 to 3 (a formulation showing no turbidity corresponds to a visual score 0, and a formulation showing visual turbdity in daylight corresponds to visual score 3). A formulation is classified physical unstable v, th respect to protein aggregation, when it shows visual turbidity in daylight. Alternatively, the turbidity of the formulation can be evaluated by simple turbidity measurements we -known to the skilled person. Physical stability of the aqueous protein formulations can a so be evaluated by using a spectroscopic agent or probe of the conformational states of the protein. The probe is preferably a small molecule that preferentially binds :o a non-native conformer of the protein. One example of a small molecular spectroscopic probe of protein structure is Thioflavin T. Thioflavin T is a fluorescent dye that has been widely used for the detection of amyloid fibrils. In the presence of fibrils, and perhaps other protein configurations as well. Thioflavin T gives rise to a new excitation maximum at about 450 nm and enhanced emission at about 482 nm when bound to a fibril protein form. Unbound Thioflavin T is essentially non-fluorescent at the wavelengths. Other small molecules can be used as probes of the changes in protein structure from native to non-native states. For instance the "hydrophobic patch" probes that bind preferentially to exposed hydrophobic patches of a protein. The hydrophobic patches are generally buried within the tertiary structure of a protein in its native state, but become exposed as a protein begins to unfold or denature. Examples of these small molecular, spectroscopic probes are aromatic, hydrophobic dyes, such as antrhacene, acridine, phenanthroline or the like. Other spectroscopic probes are metal-amino acid complexes, such as cobalt metal complexes of hydrophobic amino acids, such as phenylalanine, leucine, isoleucine, methionine, and valine, or the like. The term "chemical stability" of the protein formulation as used herein refers to chemical covalent changes in the protein structure leading to formation of chemical degradation products with potential less biological potency and/or potential increased immunogens properties comparer! to the native protein structure. Various chemical degradation products can be formed depending on the type and nature of the native protein and the environment to which the protein is exposed. Elimination of chemical degradation can most probably not be completely avoided and increasing amounts of chemical degradation products is often seen during storage and use of the protein formulation as well-known by the person skilled in the art. Most proteins are prone to deamidation, a process in which the side chain amide group in glutaminyl or asparaginyl residues is hydrolysed to form a free carboxylic acid. Other degradations pathways involves formation of high molecular weight transformation products where two or more protein molecules are covalently bound to each other through transamidation and/or disulfide interactions leading to formation of covalently bound dimer, oligomer and polymer degradation products (Stability of Protein Pharmaceuticals, Ahem. T.J. & Manning M.C., Plenum Press, New York 1992). Oxidation (of for instance methionine residues) can be mentioned as another variant of chemical degradation. The chemical stability of the protein formulation can be evaluated by measuring the amount of the chemical degradation products at various time-points after exposure to different environmental conditions (the formation of degradation products can often be accelerated by for instance increasing temperature). The amount of each individual degradation product is often determined by separation of the degradation products depending on molecule size and/or charge using various chromatography techniques (e.g. SEC-HPLC and/or RP-HPLC). Hence, as outlined above, a "stabilized formulation" refers to a formulation with increased physical stability, increased chemical stability or increased physical and chemical stability. In general, a formulation must be stable during use and storage (in compliance with recommended use and storage conditions) until the expiration date is reached. In one embodiment of the invention the pharmaceutical formulation comprising the compound according to the present invention is stable for more than 6 weeks of usage and for more than 3 years of storage. In another embodiment of the invention the pharmaceutical formulation comprising the compound according to the present invention is stable for more than 4 weeks of usage and for more than 3 years of storage. In a further embodiment of the invention the pharmaceutical formulation comprising the compound according to the present invention is stable for more than 4 weeks of usage and for more than two years of storage. In an even further embodiment of the invention the pharmaceutical formulation comprising the compound is stable for more than 2 weeks of usage and for more than two years of storage. In another aspect the present invention relates to the use of a compound according to the invention for the preparation of a medicament. In one embodiment of the invention a compound according to the invention wherein the therapeutic agent is a GLP-1 peptide is used for the preparation of a medicament for the treatment or prevention of hyperglycemia, type 2 diabetes, impaired glucose tolerance, type 1 diabetes, obesity, hypertension, syndrome X, dyslipidemia.disorders associated with toxic hypervolemia, cognitive disorders, atherosclerosis, myocardial infarction, coronary heart disease, stroke and other cardiovascular disorders, inflammatory bowel syndrome, dyspepsia and gastric ulcers. In another embodiment of the invention a compound according to the invention wherein the therapeutic agent is a GLP-1 peptide is used for the preparation of a medicament for delaying or preventing disease progression in type 2 diabetes. In another embodiment of the invention a compound according to the invention wherein the therapeutic agent is a GLP-1 peptide is used for the preparation of a medicament for decreasing food intake, decreasing (3-cell apoptosis, increasing fi-cell function and p-cell mass, stimulating p-celi regeneration, and/or for restoring glucose sensitivity to p-cells. In another embodiment the present invention relates to the use of a compound according to the invention wherein the therapeutic agent is a GLP-2 peptide for the preparation of a medicament for the treatment of small bowel syndrome, inflammatory bowel syndrome or Crohns disease. In another embodiment the present invention relates to the use of a compound according to the invention wherein the therapeutic agent is an insulin peptide for the preparation of a medicament for the treatment of hyperglycemia, type 1 diabetes, type 2 diabetes or p-cell deficiency. The treatment with a compound according to the present invention may also be combined with combined with a second or more pharmacologically active substances, e.g. selected from antidiabetic agents, antiobesity agents, appetite regulating agents, antihypertensive agerr.s. 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, GLP-1 agonists, sulphonylureas, biguanides, meglitinides, glucosidase inhibitors, glucagon antagonists, DPP-IV (dipeptidyl peptidase-IV) inhibitors, 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), compounds lowering food intake, RXR agonists and agents acting on the ATP-dependent potassium channel of the p-cells; Cholestyramine, colestipol, clofibrate, gemfibrozil, lovastatin, pravastatin. simvastatin, probucol, dextrothyroxine, neteglinide, repaglinide; [3-blockers such as alprenolol, atenolol, timolol, pindolol, propranolol and metoprolol, ACE (angiotensin converting enzyme) inhibitors such as benazepril, captopril, enalapril, fosinopril, lisinopril, alatriopril, qu;napril and ramipril, calcium channel blockers such as nifedipine, felodipine, nicardipine, isradipine, nimodipine, diltiazem and verapamil, and a-blockers such as doxazosin, urapidil, prazosin and terazosin; CART (cocaine amphetamine regulated transcript) agonists, NPY (neuropeptide Y) antagonists, MC4 (melanocortin 4) agonists, orexin antagonists, TNF (tumor necrosis factor) agonists, CRF (corticotropin releasing factor) agonists, CRF BP (corticotropin releasing factor binding protein) antagonists, urocortin agonists, p3 agonists, 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 [5 agonists; histamine H3 antagonists, gastrin and gastrin analogs. It should be understood that any suitable combination of the compounds according to the invention with one or more of the above-mentioned compounds and optionally one or more further pharmacologically active substances are considered to be within the scope of the present invention. The present invention is further illustrated by the following examples which, however, are not to be construed as limiting the scope of protection. The features disclosed in the foregoing description and in the following examples may, both separately and in any combination thereof, be material for realising the invention in diverse forms thereof. EXAMPLES In the examples the following terms are intended to have the following, general meanings: Boc: tert-butyloxycarbonyl Bt: 1-benzotriazolyl DBU: 1,8-diazabicyclo[5.4.0]undec-7-ene DCM: dichloromethane, methylenechloride Dde: 1-(4,4-dimethyl-2,6-dioxocyclohexylidene)ethyl DIG: diisopropylcarbodiimide DMA: N,N-dimethylacetamide DMF: N,N-dimethylformamide DMSO: dimethyl sulfoxide DMAP: 4-dimethylaminopyridine DMPU: 1,3-dimethyltetrahydropyrimidin-2-one EDC or EDAC N-ethyl-N'-(3-dimethylaminopropyl)carbodiimide hydrochloride Fmoc: 9-fluorenylmethyloxycarbonyl HBTU: 2-(1H-Benzotriazol-1-yl-)-1,1,3,3 tetramethyluronium hexafluorophosphate HOAt: 3-hydroxy-3H-[1,2,3]triazolo[4,5-b]pyridine, 4-aza-3-hydroxybenzotriazole HOBt: N-hydroxybenzotriazole, 1-hydroxybenzotriazole HONSu: N-hydroxysuccinimide NMP: N-methylpyrrolidone HPLC: high pressure liquid chromatography Pmc 2,2,5.7,8-pentamethylchroman-6-sulfonyl r.t. room temperature Su: succinimidyl TIS triisopropylsilane Trt: trityl. triphenylmethyl Ts: toluenesulfonyl TSTU O-(1 -succinimidyl)-N,N,N',N'-tetramethyluronium hexafluorophosphate DIEA diisopropylethylamine H2O water CH3CN acetonitrile OtBu tert butyl ester tBu tert butyl Trt triphenylmethyl Pmc 2,2,5,7,8-Pentamethyl-chroman-6-sulfonyl Dde 1 -(4,4-Dimethyl-2,6-dioxocyclohexylidene)ethyl DCM dichloromethane TFA: trifluoroacetic acid Et20: diethylether NMR spectra were recorded on Bruker 300 MHz and 400 MHz instruments. HPLC-MS was performed on a Perkin Elmer instrument (API 100). HPLC-systems from Merck-Hitachi (Hibar™ RT 250-4, Lichrosorb™ RP 18, 5.0 prn, 4.0 x 250 mm, gradient elution, 20% to 80% acetonitrile in water within 30 min, 1.0 ml min, detection at 254 nm) and Waters (Symmetry™, C18, 3.5 pm, 3.0 x 150 mm, gradient elution, 5% to 90% acetonitrile in water within 15 min, 1.0 ml/min, detection at 214 nm) v.ere used. Furthermore, where stated the following HPLC method h8 was used: The reverse phase analysis was performed using UV detections at 214, 254, 276 and 301 nm on a 218TP54 4.6 mm x 150 mm C-18 silica column, which was eluted at 1 ml/min at 42 °C. The column was equilibrated with 5% acetonitrile, 85% water and 10% of a solution of 0.5% trifluoroacetic acid in water and eluted by a linear gradient from 5% acetonitrile, 85% water and 10% of a solution of 0.5% trifluoroacetic acid to 90% acetonitrile and 10% of a solution of 0.5% trifluoroacetic acid over 15 min. Furthermore, where stated the following HPLC method A was used: The RP-analysis was performed using a Waters 2690 systems fitted with a Waters 996 diode array detector. UV detections were collected at 214, 254, 276, and 301 nm on a 218TP54 4.6 mm x 250 mm 5u C-18 silica column (The Seperations Group, Hesperia), which was oluted at 1 ml/min at 42°C. The column was equilibrated with 5% acetonitrile (+ 0.1% TFA) in an aqueous solution of TFA in water (0.1%). After injection, the sample was eluted by a gradient of 0% to 90% acetonitrile (+ 0.1% TFA) in an aqueous solution of TFA in water (0.1%) during 50 min. General procedure (A) The compounds of formula (I) according to the invention may be prepared by the general procedure (A): (I) (II) A molecule of which a prolonged halflife in plasma is required and which contains at least one acylable amino group is dissolved in a suitable solvent (water, alcohols, DMF, DMSO, DMPU, or mixtures thereof) and a solution or suspension of (II) in DMF or DMSO is added. The mixture is stirred at room temperature and the progress of the reaction is followed by HPLC. If the reaction proceeds too slowly catalytic amounts of DMAP may be added. The product is isolated by preparative HPLC of the whole reaction mixture. General procedure (B) The compounds of formula (II) according to the invention may be prepared by the general procedure (B): A -(5-tetrazolyl)alkanoic acid or ester. In the case of the ester, it is converted to the acid by treatment with an excess of NaOH or KOH in a mixture of water and an alcohol. Evaporation of the alcohol and addition of dilute aqueous HCI yields the o>-(5-tetrazolyl)alkanoic acid, which can be isolated by filtration. Alternatively, the general procedure (B) may also be conducted with an co-halo alkanoic ester instead of an acid. Saponification of the resulting co-(tetrazol-5-yl)alkanoic ester to the corresponding acid can be performed by treatment with an excess KOH or NaOH in a mixture of water and ethanol. General procedure (C) The compounds of formula (II) according to the invention may also be prepared by the general procedure (C): An fo-(5-tetrazolyl)alkanoic acid is converted into an acyl halide or N-hydroxysuccinimidyl ester, and then coupled to lysine methyl ester. Saponification of the resulting product yields N,N'-bis(o>-(5-tetrazolyl)alkanoyl)lysine. General procedure (D) The compounds of formula (II) according to the invention may also be prepared by the general procedure (Di A w-haloalkanoic acid or ester is treated with a cyanophenol, cyanothiophenol, dicyanophenol, cyanobiphenylol, cyanoterphenylol, cyanoaniline, cyanohydroxyheteroarene, or a related reagent containing at least one cyano group and one arene- or heteroarene- bound hydroxyl group in the presence of a base such as K2C03 or DBU in a suitable solvent, such as DMF, DMSO, acetone, or an alcohol until complete conversion to the aryl or heteroarylether, -thioether, or -amine has taken place. The reaction is followed by analyzing samples by 1H NMR. The resulting co-aryloxy-, co-arylthio-, or w-arylaminoalkanoic acid or ester is isolated by dilution with water and extraction with AcOEt or DCM. Treatment of this product with NaN3 in the presence of AcOH and NEt3 in DMF at 140 °C until all the starting material is consumed (as determined by 1H NMR) yields the corresponding co-(5-tetrazolyl)aryloxy-, o-(5-tetrazolyl)arylthio-, or o>-(5-tetrazolyl)arylaminoalkanoic acid or ester. In the case of the ester, it is converted to the acid by treatment with an excess of NaOH or KOH in a mixture of water and an alcohol. Evaporation of the alcohol and addition of dilute aqueous HCI yields the -(5-tetrazolyl)alkanoyl)sulfamoyl)butyric acid methyl ester is saponified to the corresponding acid by treatment with an excess of KOH or NaOH in a mixture of water and methanol. General procedure (F): Solid phase synthesis, purification and characterization of peptides and derivatized peptides: The peptides were synthesized on Fmoc protected Rink amide resin (Novabiochem), Fmoc protected Wang resin or chlorotrityl resin using Fmoc strategy on an Applied Biosystems 433A peptide synthesizer in 0.25 mmol scale using the manufacturer supplied FastMoc UV protocols which employ HBTU mediated couplings in NMP and UV monitoring of the deprotection of the Fmoc protection group. The protected amino acid derivatives used were standard Fmoc-amino acids (Anaspec) supplied in preweighed cartridges suitable for the ABI 433A synthesizer with the exception of unnatural aminoacids such as Fmoc-Aib-OH (Fmoc-aminoisobutyric acid), The attachment of sidechains and linkers to specific lysine residues on the crude resin bound protected peptide was carried out in a specific position by incorporation of Fmoc-Lys(Dde)-OH during automated synthesis followed by selective deprotection with hydrazine. Procedure for removal of Dde-protection. The resin (0.25 mmol) was placed in a manual shaker/filtration apparatus and treated with 2% hydrazine in NMP (20 ml, 2 x 12 min) to remove the DDE group and wash with NMP (4x20 ml). Procedure for attachment of sidechains to Lysine residues. The amino acid (4 molar equivalents relative to resin) was dissolved in NMP (10 ml). HOBt (4 molar equivalents relative to resin) and diisopropylcarbodiimide (4 molar equivalents relative to resin) were added and the solution was stirred for 15 min. The solution was added to the resin and DIPEA (4 molar equivalents relative to resin) was added. The resin was shaken 24 hours at room temperature. The resin was washed with NMP (2 x 20 ml), NMR/DCM (1:1; 2 x 20ml) and DCM (2 x 20 ml). Procedure for removal of Fmoc-protection: The resin (0.25 mmol) was placed in a filter flask in a manual shaking apparatus and treated with NMP/DCM (1:1) (2 x 20 ml) and with NMP (20 ml), a solution of 2C% piperidine in NMP (3 x 20 ml, 10 min each). The resin was washed with NMP (2 x 20 ml). NMP/DCM (1:1) (2 x 20ml) and DCM (2 x 20 ml). Procedure for cleaving the peptide from the resin: The peptide was cleaved from the resin by stirring for 180 min at room temperature with a mixture of TFA, water and triisopropylsilane (95:2.5:2.5). The cleavage mixture was filtered and the filtrate was concentrated to an oil by a stream of nitrogen. The crude peptide was precipitated from this oil with 45 ml diethyl ether and washed 3 times with 45 ml diethyl ether. Purification: The crude peptide was purified by semipreparative HPLC on a 25 mm x 250 mm column packed with 5j.i C-18 silica. After drying the crude peptide was dissolved in 5 ml 50% acetic acid H2O and diluted to 20 ml with H2O and injected on the column which then was eluted with a gradient of 40-60 % CH3CN in 0.1% TFA 10 ml/min during 50 min at 40 °C. The peptide containing fractions were collected. The purified peptide was lyophilized after dilution of the eluate with water. The final product obtained was characterised by analytical RP-HPLC (retention time) and by LCMS The RP-HPLC analysis was performed using UV detection at 214 nm and a Vydac 218TP54 4.6 mm x 250 mm 5|.i C-18 silica column (The Separations Group, Hesperia, USA) which was eluted at 1 ml/min at 42 =C. Two different elution conditions were used: A1: Equilibration of the column with in a buffer consisting of 0.1M (NH4)2SO4, which was adjusted to pH 2.5 with concentrated H2SO4 and elution by a gradient of 0% to 60% CH3CN in the same buffer during 50 min. B1: Equilibration of the column with 0.1 % TEA / H2O and elution by a gradient of 0% CH3CN / 0.1% TFA / H2O to 60% CH3CN / 0.1% TFA / H2O during 50 min. B6: Equilibration of the column with 0.1% TFA / H2O and elution by a gradient of 0% CH3CN / 0.1% TFA / H2O to 90% CH3CN / 0.1% TFA / H2O during 50 min. LCMS was performed on a setup consisting of Hewlett Packard series 1100 G1312A Bin Pump, Hewlett Packard series 1100 Column compartment, Hewlett Packard series 1100 G1315A DAD diode array detector, Hewlett Packard series 1100 MSD and Sedere 75 Evaporative Light Scattering detectorcontrolled by HP Chemstation software. The HPLC pump is connected to two eluent reservoirs containing: A: 10mM NH4OH in water B: 10mM NH4OH in 90% acetonitrile The analysis was performed at 23 °C by injecting an appropriate volume of the sample (preferably 20 j.il) onto the column which is eluted with a gradient of A and B. The HPLC conditions, detector settings and mass spectrometer settings useo are giving in the following table. Column: Waters Xterra MS C-18 X 3 mm id 5 urn Gradient: 5% -100% acetonitrile linear during 6.5 min at 1.5ml/min Detection: 210 nm (analogue output from DAD) ELS: analogue output from ELS MS ionisation mode API-ES. Scan 100-1000 amu step 0.1 amu Typical Procedure: A resin (Fmoc-Gly-Wang resin, 0.6 mmol/g Novabiochem 0.25 mmole) was used to produce the primary sequence on an ABI 433A machine according to manufacturers guidelines. The resin (0.25 mmole) was placed in a manual shaker/filtration apparatus and treated with 2% hydrazine in NMP in (2x12 min. 2x20 ml) to remove the Dde group. The resin was washed with NMP (4x20 ml). Fmoc-8-amino-3,6-dioxaoctanoic acid (Neosystem FA03202) (4 molar equivalents relative to resin) was dissolved in NMP/DCM (1:1, 20 ml). HOBt (4 molar equivalents relative to resin) and DIG (4 molar equivalents relative to resin) was added and the solution was stirred for 15 min. The solution was added to the resin and DIPEA (4 molar equivalents relative to resin) was added. The resin was shaken 24 hours at room temperature. The resin was washed with NMP (4x20 ml). A solution of 20% piperidine in NMP (3x20 ml, 10 min each) was added to the resin while shaking. The resin was washed with NMP (4x20 ml). 16-(Tetrazol-5-yl)hexadecanoyl-ONSu ester (4 molar equivalents relative to resin) was dissolved in NMP (20 ml). The solution was added to the resin and DIPEA (4 molar equivalents relative to resin) was added. The resin was shaken 24 hours at room temperature. The resin was washed with NMP (2x20 ml), NMP/DCM (1:1) (2x20ml) and DCM (2x20 ml). The peptide was cleaved from the resin by stirring for 180 rnin at room temperature with a mixture of TFA, water and triisopropylsilane (95:2.5:2.5, 15 ml). The cleavage mixture was filtered and the filtrate was concentrated to an oil in vaccuum. The crude peptide was precipitated from this oil with 45 ml diethyl ether and washed 3 times with 45 ml diethyl ether. The crude peptide was purified by preparative HPLC on a 20 mm x 250 mm column packed with 7n C-18 silica. The crude peptide was dissolved in 5 ml 50% acetic acid in water and diluted to 20 ml with H2O and injected on the column which then was eluted with a gradient of 40-60 % (CH3CN in water with 0.1% TFA) 10 ml/min during 50 min at 40 °C. The peptide containing fractions were collected. The purified peptide was lyophilized after dilution of the eluate with water. Radioligand binding to plasma membranes expressing the human GLP-1 receptor The binding assay was performed with purified plasma membranes containing the human GLP-1 receptor. The plasma membranes containing the receptors were purified from stably expressing BHK tk-ts 13 cells. The membranes were diluted in Assay Buffer (50 mM HEPES, 5 mM EGTA, 5 mM MgCI2, 0.005% Tween 20, pH=7.4) to a final concentration of 0.2 mg/ml of protein and destributed to 96-well microtiter plates precoated with 0.3 % PEL Membranes in the presence of 0.05 nM [125I]GLP-1, unlabelled ligands in increasing concentrations and different HSA concentrations (0.005%, 0.05%, and 2%) were incubated 2 hr at 30°C. After incubation, unbound ligands were separated from bound ligands by filtration through a vacuum-manifold followed by 2X100 /j\ washing with ice cold assaybuffer. The filters were dried overnight at RT, punched out and quantified in a y-counter. Example 1. 1 6-(5-tetrazolyl)hexadecanoic acid 33 A mixture of 16-bromohexadecanoic acid (16.61 g, 49.5 mmol), DMSO (150 ml), NaCN (12.5 g, 255 mmol), and Nal (1.92g, 12.8 mmol) was stirred at 120 °C for 20 h. The mixture was allowed to cool to room temperature, and was then poured into a stirred mixture of water (1.7 I) and concentrated HCI (30 ml). Rinsing with water (100 ml). The resulting suspension was stirred at room temperature overnight. The product was filtered and washed with water (2 x 100 ml), and the solid was recrystallized twice from MeCN (90 ml and 50 ml). 10.1 g (72%) of 16-cyanohexadecanoic acid was obtained. 1H NMR (DMSO) 8 1.20-1.39 (m, 22H), 1.50 (m, 4H), 2.18 (t, J = 7 Hz, 2H), 2.48 (t, J = 7 Hz, 2H), 11.95 (s, 1H). This product was mixed with DMF (150 ml), AcOH (10.0 ml, 174.8 mmol), NEt3 (25 ml, 180 mmol), and NaN3 (11.83 g, 182 mmol), and the mixture was stirred at 120 °C for 80 h, while following the conversion by 'H NMR. The mixture was concentrated under reduced pressure, and to the residue water (250 ml) and concentrated HCI (25 ml) were added. The acidic mixture was stirred at room temperature for 2 d, filtered, and the solid recrystallized from MeCN (approx 300 ml). 7.60 g (65%) of the title compound was obtained. 1H NMR (DMSO) 5 1.24 (m, 22H), 1.48 (m, 2H), 1.68 (m, 2H), 2.18 (t, J = 7 Hz, 2H), 2.84 (t, J = 7 Hz, 2H), 11.95(s, 1H). Example 2. 4-(N-(16-(5-tetrazolyl)hexadecanoyl)sulfamoyl)butyric acid To a suspension of 16-(5-tetrazolyl)hexadecanoic acid (3.25 g, 10.0 mmol) in DCM (40 ml) was added oxalyl chloride (1.2 ml, 14.0 mmol). The mixture was stirred at room temperature for 42 h, concentrated, coevaporated once with PhMe, and to the residue were added a solution of methyl 4-sulfamoyl butyrate (1.66 g, 9.16 mmol) in DCM (35 ml) and then DMAP (3.67 g, 30.0 mmoH. The heterogenous mixture was stirred at room temperature for 6.5 h and then concentrated. To the residue was added a mixture of water (50 ml) and 1N HCI (50 ml), and the resulting mixture was stirred at room temperature for 5 d. The product was filtered, washed with water (100 ml), and recyrstallized from MeCN (25 ml), to yield 1.84 g (41%) of the N-acylsulfonamide methyl ester. To this ester (1.06 g, 2.17 mmol) in MeOH (15 ml) was added a solution of NaOH (0.38 g, 9.5 mmol, 4.4 eq) in water (1.5 ml). After stirring at room temperature for 1.5 h the mixture was poured into a mixture of water (80 ml) and 1N HCI (20 ml). The mixture was stirred for 3 h, filtered, and the product was dried under reduced pressure. 1.09 g (100%) of the title compound was obtained. 1H NMR (DMSO) 5 1.24 (m, 20H), 1.49 (m, 4H), 1.69 (m, 2H), 1.85 (m, 2H), 2.27 (t, J = 7 Hz, 2H), 2.39 (t, J = 7 Hz, 2H), 2.86 (t, J = 7 Hz, 2H), 3.38 (m, 2H), 11.59 (s, 1 H). A mixture of 16-bromohexadecanoic acid (15.5 g, 46.2 mmol), MeOH (100 ml), PhMe (30 ml), trimethylorthoformate (30 ml), and polystyrene-bound benzenesulfonic acid (3.6 g) was stirred at 55 °C. After 69 h the mixture was filtered through celite and the filtrate was concentrated to yield 16.85 g of an oil (100% yield). (4'-Cyanobiphenyl-4-yloxy)hexadecanoic acid methyl ester: A mixture of 16-bromohexadecanoic acid methyl ester (4.86 g, 13.9 mmol), MeCN (20 ml), 4-cyano-4'-hydroxybiphenyl (3.16 g, 16.2 mmol), and K2CO3 (2.45 g, 17.7 mmol) was stirred at 82 °C. After 17 h satd aquous NaHCO3 (150 ml) was added, and the product was filtered, washed with water, and recrystallized from boiling MeCN (approx 80 ml). Filtration and drying under reduced pressure yielded 5.40 g (84%) of (4'-cyanobiphenyI-4-yloxy)hexadecanoic acid methyl ester colorless needles. 16-(4'-(5-Tetrazolyl)biphenyl-4-yloxy)hexadecanoic acid methyl ester: A mixture of (4'-cyanobiphenyl-4-yloxy)hexadecanoic acid methyl ester (2.75 g, 5.93 mmol), DMF (7.0 ml), NEt3 (4.0 ml, 28.9 mmol), AcOH (1.75 ml, 29.1 mmol), and NaN3 (2.50 g, 38.5 mmol) was stirred at 140 °C. After 17 h water (50 ml) and 1N HCI (50 ml) were added, followed by acidification with cone. HCI (approx 2 ml). The product was filtered and recrystallized from MeCN/PhMe (approx 60 + 60 ml). Filtration and drying under reduced pressure yielded 2.87 g (96%) of 16-(4'-(5-tetrazolyl)biphenyl-4-yloxy)hexadecanoic acid methyl ester. 16-(4'-(5-Tetrazolyl)biphenyl-4-yloxy)hexadecanoic acid: A mixture of 16-(4'-(5-tetrazolyl)biphenyl-4-yloxy)hexadecanoic acid methyl ester (2.87 g, 5.66 mmol), MeOH (30 ml), and a solution of NaOH (1.51 g, 37.8 mmol) in water (2.0 ml) was stirred at 70 °C. After 4 d water (100 ml) and 1N HCI (50 ml) were added, and the product was filtered, washed with water, coevaporated with MeCN/PhMe, and dried under reduced pressure. 2.68 g (96%) of 16-(4'-(5-tetrazolyl)biphenyl-4-yloxy)hexadecanoic acid was obtained. 1H NMR (DMSO) 6 1.20-1.50 (m, 24H), 1.72 (m, 2H), 2.18 (t, J = 7 Hz, 2H), 4.02 (t, J = 6 Hz, 2H), 7.04 (d, J = 8 Hz, 2H), 7.71 (d, J = 8 Hz, 2H), 7.87 (d, J = 8 Hz, 2H), 8.09 (d, J = 8 Hz, 2H), 11.95(brs, 1H). Example 4.4-(4-(5-Tetrazolyl)-[1,1',4',1"]-terphenyl-4"-yloxy)butyric acid 4-(4'-Bromobiphenyl-4-yloxy)butyric acid ethyl ester: A mixture of 4-(4-bromophenyl)phenol (3.74 g, 15.0 mmol), MeCN (20 ml), ethyl 4- bromobutyrate (4.42 g, 22.7 mmol), and K2C03 (3.12 g, 22.6 mmol) was stirred at 80 °C. *"- After 16 h water (100 ml) and 1N HCI (40 ml) were added, and the product was extracted (3 x AcOEt), the combined extracts were washed with brine (2 x), dried (MgSO4), and concentrated. The residue was recrystallized from EtOH (40 ml) to yield 4.35 g (80%) of 4-(4'-bromobiphenyl-4-yloxy)butyric acid ethyl ester as colorless plates. 4-(4-Cyano-[1,1',4',1"]-terphenyl-4"-yloxy)butyric acid ethyl ester: To 4-(4'-bromobiphenyl-4-yloxy)butyric acid ethyl ester (2.03 g, 5.59 mmol) in toluene (30 ml) and EtOH (20 ml) were added triphenylphosphine (0.17 g, 0.65 mmol), 4-cyanophenylboronic acid (1.23 g, 8.37 mmol), Pd(OAc)2 (65 mg, 0.29 mmol), and a solution of Na2CO3 (2.33 g, 22.0 mmol) in water (10 ml). The mixture is stirred at 70 °C (oil-bath temperature). After 66 h water (100 ml) and 1N HCI (50 ml) were added and the product was extracted (3 x DCM). The combined extracts were washed with water, then with satd. aqueous NaHCO3, dried and concentrated to yield 2.33 g of a gray solid, which is washed with hot EtOH and dried under reduced pressure to yield 0.81 g (38%) of 4-(4-cyano- [1l1l,4',rHerphenyl-4"-yloxy)butyric acid ethyl ester. From the ethanol washings more product (0.48 g, 22%) precipitated. 4-(4-(5-Tetrazolyl)-[1,1',4',1"]-terphenyl-4"-yloxy)butyric acid ethyl ester: A mixture of 4-(4-cyano-[1,1',4',1"]-terphenyl-4"-yloxy)butyric acid ethyl ester (1.29 g, 3.35 mmol), DMF (4.0 ml), NEt3 (2.3 ml, 16.6 mmol), AcOH (1.0 ml, 16.7 mmol), and NaN3 (1.32 g, 20.3 mmol) was stirred at 140 °C. After 20 h water (50 ml) and 1N HCI (50 ml) were added and the product is isolated by filtration, washed with hot MeCN and dried under reduced pressure to yield 1.16 g (81%) of 4-(4-(5-tetrazolyl)-[1,1',4',1"]-terphenyl-4"-yloxy)butyric acid ethyl ester as a gray solid. 4-(4-(5-Tetrazolyl)-[ 1.1 ',4', 1 "]-terphenyl-4"-yloxy)butyric acid A heterogenous mixture of 4-(4-(5-tetrazolyl)-[1,1',4',1"]-terphenyl-4"-yloxy)butyric acid ethyl ester (1.16 g, 2.71 mmol), EtOH(10ml), NaOH(0.75g, 18.8 mmol), and water (1.5 ml) was stirred at 80 °C. After 18 h water (50 ml) and 1N HCI (50 ml) were added. After stirring for 0.5 h the product was filtered, washed with water, and the solid was coevaporated with MeCN and PhMe to yield 0.79 g (73%) of 4-(4-(5-tetrazolyl)-[1,1',4M"]-terphenyl-4"- yloxy)butyric acid as a light-brown powder. 1H NMR (DMSO) 5 1.98 (quint, J = 7 Hz, 2H), 2.41 (t, J = 7 Hz, 2H), 4.03 (t, J = 7 Hz, 2H), 7.04 (d, J = 8 Hz, 2H), 7.69 (d, J = 8 Hz, 2H), 7.77 (d, J = 8 Hz, 2H), 7.85 (d, J = H Hz, 2H), 7.98 (d, J = 8Hz, 2H). 8.14 (d, J = 8 Hz. 2H), 12.19 (brs, 1H). Example 5 N-e-26-(16-[5-tetrazolyl]hexadecanoyl)Arg34GLP-1-(7-37) - This compound was prepared by acylation with 16-[5-tetrazolyl]hexadecanoic acid (Example 1) of unprotected Arg34GLP-1-(7-37) peptide in solution. The succinimidyl ester of 16-[5- tetrazolyljhexadecanoic acid was prepared by mixing the acid (29 mg) with THF (0.9 ml), DIPEA (17 micro-liter), and TSTU (30 mg), and stirring the resulting mixture at room temperature for 1 h. Arg34GLP-1-(7-37) (0.33 g, 30% pure) was dissolved in water (5 ml) and DIPEA (50 microliter), and the solution of the succinimidyl ester (0.3 ml) was added. After stirring at room temperature for 20 min the excess succinimidyl ester was quenched by addition of an excess glycine, and the product was purified by preparative HPLC. 38 mg of the title compound were obtained. HPLC: (method B6): RT= 9.36 min (100%) LCMS: m/z = 1231 (MH33+). Calculated for (MH33+): 1231 Examples Gly8,Arg2634GLP-1(7-37)Lys(16-(5-tetrazolyl)hexadecanoyl) Glys,Arg26'34GLP-1-(7-37) was prepared on a 433A peptide synthesizer using standard Fmoc- methodology and using Fmoc-Lys(Boc)-trityl polystyrene (0.88 g, loading: 0.79 mmol/g) as starting resin. After purification by preparative HPLC 25 mg of Gly8,Arg26|34GLP-1(7-37) peptide was obtained. The title compound was prepared by acylation of Gly8,Arg26i34GLP-1(7-37) peptide (25 mg) with 16-(5-tetrazoiyl)hexadecanoic acid (23 mg) as described for Example 5. 14.6 mg of the title compound were obtained. HPLC: (method B6Y. RT= 9.02 min (99%) LCMS: m/z = 1279 (MH^). Calculated for(MH33+): 1279 Example 7 Gly8,Arg28'34GLP-1(7-37)l_ys{4-[N-(16-{5-tetrazolyl}hexadecanoylN The title compound was prepared as Example 6 from {4-[N-(16-{5- tetrazolyl}hexadecanoyl)sulfamoyl]butyric acid (21 mg; Example 2) and Gly8,Arg2eU4GLP-1(7- 37) (25 mg). 1 .5 mg of the title compound was obtained. HPLC: (method B6): RT= 9.05 min (95%) LCMS: m/z = 1328 (MH33"). Calculated for(MH33+): 1328 Example 8 N-E-26-{4-[N-(16-{5-tetrazolyl}hexadecanoyl)sulfamoyl]butyryl}Arg34GLP-1(7-37) This compound was prepared as Example 5 from {4-[N-(16-{5- tetrazolyl}hexadecanoyl)sulfamoyl]butyric acid (21 mg; Example 2) and Arg34GLP-1(7-37) peptide (0.3 g, 30% pure). 10.1 mg of the title compound was obtained. HPLC: (method B6): RT= 9.35 min (94%) LCMS: m/z = 1281 (MH33+). Calculated for(MH33+): 1281 Example 9 N-e-37-(2-(2-(2-(16-(tetra2ol-5-yl)(hexadecanoylamino)ethoxy)ethoxy)acetyl)) Aib"-22'35Lys37GLP-1(7-37) Prepared as described in the Typical Procedure'. HPLC: (method B6): RT = 31.8 min (98%), (method A1): RT = 41.5 min LCMS: m/z = 988.7 (MH4)4+, 1317.8 (MH3)3*. Calculated (MH)+: 3949.6 Example 10 Human growth hormone (100 mg, hGH) was dissolved in H20 (6 ml), DIEA (7.5 pi), and NMP (6 ml) and cooled to 0 °C. 16-(Tetrazol-5-yl)hexadecanoyl-ONSu (3.5 mg, 2 eq), dissolved in NMP (100 pi), was added. The reaction mixture was stirred for 1 h and purified by ion exchange chromatography. Purification of monoacylated hGH in position 140 or 145. The crude reaction mixture was diluted five times in 50 mM Tris pH 8.5 and applied to a Mono Q column. For purification of 6 ml crude reaction mixture a 10 ml 10/10 Mono Q column from Amersham Pharmcia was used. A 1000 CV gradient was used to separate the native, monoacylated in position 30/45/70, monoacylated in position 140/145, diacylated and triacylated hGH. Shortly after elution of the triacylated hGH, a steep gradient was used to elute dimeric hGH. As eluting buffer 50 mM Tris, 2 M NaCI, pH 8.5 was used. The purification was performed at 4 °C. After elution, fractions containing monoacylated hGH (peak 2) was pooled and subsequently ultrafiltrated using a Amicon with a YM10 filter. The washing buffer was 50 mM Ammoniumcarbonate pH 8.0. After ultrafiltration, the acylated protein was lyophillised. Chromatograms depicting A280 nm and A254 nm both exhibited five distinct peaks which were characterised by peptide mapping : Peak 1 contains native hGH Peak 2 contains monoacylated hGH in position 38 or 45 or 70. Peak 3 contains monoacylated hGH in position 140 or 145 Peak 4 contains diacylated hGH Peak 5 contains triacylated hGH Example 11 Gly8,Glu22'2woArg16-2e-M GLP-1 (7-37)Lys(16-(1 H-tetrazol-5-yl)hexadecanoic acid [2-(2-{[2-(2-carbamoylmethoxyethoxy)ethylcarbamoyl]methoxy}ethoxy)ethyl]amide)-NH2 Prepared as described in the Typical Procedure'. HPLC: (method B6): RT = 30.283 min (96%) LCMS: m/z = 1441.8 (MH3)3+. Calculated (MH3)3*: 1439.6 Example 12 Gly8Arg26'34GLP-1(7-37)Lys(4-(4-(4-(4-(5-tetrazolyl)phenyl)phenyl)phenoxy)butyr,l) Prepared as described in the Typical Procedure'. HPLC: (method B4): RT= 10.89 min (100%) LCMS: m/z = 1304 (MH3)3+. Calculated (MH3)3*: 1304 _: f G(v8.Am26.34.Lvs381GLP-1 (7-371 oeotlde GEGTFTSDVSSYLEGQAAREF I AWLVRGR G-N [Gly8,Arg26,34,Lys38] GLP-1-(7-37) peptide was prepared on an Advanced Chemtech APEX 348 peptide synthesizer using standard Fmoc methodology and using 2-chlorotrityl chloride resin (0.400 g, loading: 1.4 mmol/g) as starting resin. Lys38 was protected as Fmoc-Lys(ivDde)-OH. IvDde was removed with 3% hydrazine and 3% piperidine in NMP for 60 min. The title compound was prepared by acylation with N-Fmoc (2-(2-aminoethoxy)ethoxy)acetic acid (0,56 mmol), followed by Fmoc-group removal and acylation with 0.62 mmol of 16-(4-(5-tetrazolyl)phenoxy)hexadecanoic acid. After cleavage from the support the peptide was purified by preparative HPLC (gradient elution 0-5 min = 30% MeCN, 5-40 min = 30-65% MeCN; Xterra prep. Ms 018). -RT = 26.1 min Maidi: m/z = 4071; Calculated: 4069.6 Example 13. N-epsilon37-(2-(2-(2-(16-(4-(5-Tetrazolvl)phenoxv)hexadecanovl)ethoxy)ethoxv)acetvl)[Aib8.22.35.Lvs37]GLP-1 (7-37) [Aib 8,22,35,Lys37] GLP-1(7-37) peptide was prepared on an Advanced ChemTech APEX 348 peptide synthesizer using standard Fmoc methodology and using 2-chlorotrityl chloride resin (0.400 g, loading: 1.4 mmol/g) as starting resin. Lys37 was protected as Fmoc- Lys(ivDde)-OH. IvDde was removed with 3% hydrazine and 3% piperidin in NMP for 60 min. After this deprotection, the resin-bound peptide was acylated with N-Fmoc (2-(2- aminoethoxy)ethoxy)acetic acid (0.59 mmol), followed by Fmoc-group removal and acylation with 0.62 mmol of 16-(4-(5-tetrazolyl)phenoxy)hexadecanoic acid. The peptide was cleaved from the support (90% TFA, 5% Tis, 2% thioanisol, 3% water, 2 h), precipitated with Et2O, lyophilized, and purified by preparative HPLC (gradient elution 0-5 min = 30% MeCN, 5-40 min = 30-65% MeCN: Xterra prep. Ms C18). RT = 26.85 min Maldi: m/z = 4042. Calculated: 4040.7 Example 14. N£38-(2-(2-(2-(16-(Tetrazol-5-yl)hexadecanoyl)ethoxy)ethoxy)acetyl) [Aib8,Arg26,34,Lys38]GLP-1 (7-37) peptide (Aib8,Arg26,34,Lys38]GLP-1(7-37) peptide was prepared on the Advanced ChemTech APEX 348 peptide synthesizer using standard Fmoc methodology and 2-chlorotrityl chloride resin (0.150 g, loading: 1.4 mmol/g) as starting resin. Lys38 was protected as Fmoc-Lys(ivDde)-OH. IvDde was removed with 3% hydrazine and 3% piperidin in NMP for 60 min. After this deprotection, the resin-bound peptide was acylated with N-Fmoc (2-(2-aminoethoxy)ethoxy)acetic acid (0.35 mmol), followed by Fmoc-group removal and acylation with 0.32 mmol of 16-(5-tetrazolyl)hexadecanoic acid. The peptide was cleaved from the support (90% TFA. 5% Tis, 2% thioanisol, 3% water, 2 h), precipitated with Et2O, lyophilized, and purified by preparative RP-HPLC (gradient elution 0-5 min: 80% A, 20% B; 5-45 min to 40% A, 60% B; A: water + 0.1% TFA; B: MeCN + 0.07% TFA). LCMS: 4005. Calculated: 4005.6 Example 15. Nt38.(4-(N-(16-(Tetra2ol-5-yl)hexadecanoyl)sulfamoyl)butyryl)[Aib8,Arg26,34,Lys38]GLP-1(7-37) peptide The title compound was prepared as example 6. 8 mg of the title compound was obtained. RT: 32 min. Maldi: m/z = 4007. Calculated: 4009 Example 16. N-epsilon32-(4-[N-(16-{5-Tetrazolyl}hexadecanoyl)sulfamoyl]butyryl)-[Lys32]Exendin[1-39] peptide [Lys32]Exendin[1-39] peptide was prepared on the Advanced ChemTech APEX 348 peptide synthesizer using standard Fmoc methodology and 2-chlorotrityl chloride resin (0.150 g, loading: 1.4 mmol g) as starting resin. Lys38 was protected as Fmoc-Lys(ivDde)-OH. IvDde protection v.as removed with 3% hydrazine and 3% piperidin in NMP for 60 min. After this deprotection, the resin-bound peptide was acylated with N-Fmoc (2-(2- aminoethoxy)ethoxy)acetic acid (0.35 mmot), followed by Fmoc-group removal and acylation with 0.32 mmol of 4-(16-(5-tetrazolyl)hexadecanoyl)sulfamoylbutyric acid. The peptide was cleaved from the support (90% TFA, 5% Tis, 2% thioanisol, 3% water, 2 h), precipitated with Et2O, lyophilized, and purified by preparative RP-HPLC (gradient elution 0-5 min: 80% A, 20% B; 5-45 min to 40% A, 60% B; A: water + 0.1% TFA; B: MeCN + 0.07% TFA). Example 17 N-epsilon37-(16-(4'-(Tetrazol-5-yl)biphenyl)-4-yloxy)hexadecanoyl) [3-(4-imidazolyl)propionyl7,Aib22,35,Arg26,34,Lys37]GLP-1 (7-37) peptide [3-(4-lmidazolyl)Propionyl7,Aib22,35,Arg26,34,Lys37]GLP-1 (7-37) peptide was prepared on a 433A peptide synthesizer using standard Fmoc-methodology and using Fmoc-Lys(Boc)- trityl polystyrene (0.51 g, loading: 0.50 mmol/g) as starting resin. After purification by preparative HPLC 159 mg of [3-(4-imidazolyl)propionyl7,Aib22,35lArg26,34,Lys37]GLP-1 (7- 37) peptide was obtained. The title compound was prepared by acylation of [3-(4- imidazolyl)propionyl7,Aib22,35,Arg26,34,Lys37]GLP-1 (7-37) peptide (18 mg) with 16-(4'- (tetrazol-5-yl)biphenyl)-4-yloxy)hexadecanoic acid (10 mg) as described for Example 5. 4.74 mg of the title compound was obtained. HPLC: (method B6): RT = 38.4 min (97%) LCMS: m/z = 1333.7 (MH33*). Calculated for (MH33*): 1334.2 Example 18 N-epsilon37-(16-(Tetrazol-5-yl)hexadecanoyl) [3-(4-imidazolyl)propionyl7.Aib22,35,Arg26,34,Lys37]GLP-1 (7-37) [3-(4-lmidazolyl)proptonyl7,Aib22,35,Arg26,34,Lys37]GLP-1 (7-37) peptide was prepared as described in Example 17. The title compound was prepared by acylation of [3-{4- imidazolyl)propionyl7,Aib22,35,Arg26,34,Lys37]GLP-1 (7-37) peptide (18 mg) with 16- (tetrazol-5-yl)hexadecanoic acid (8.5 mg) as described for Example 5. 7.32 mg of the title compound was obtained. HPLC: (method B6): RT= 33.0 min (100%) LCMS: m/z = 1277.9 (MH33+). Calculated for (MH33*): 1277.8 Example 19N-epsilon37-(16-(4-(Tetrazol-5-yl)phenoxy)hexadecanoyl) [3-(4-imidazolyl)propionyl7,Aib22,35,Arg26,34,Lys37]GLP-1 (7-37) - [3-(4-lmidazolyl)propionyl7,Aib22,35,Arg26,34,Lys37]GLP-1 (7-37) peptide was prepared as described in example 17. The title compound was prepared by acylation of [3-(4-imidazolyl)propionyl7,Aib22,35,Arg26,34,Lys37]GLP-1 (7.37) peptide (18 mg) with 16-(4- (tetrazol-5-yl)phenoxy)hexadecanoic acid (8.0 mg) as described for Example 5. 2.59 mg of the title compound was obtained. HPLC: (method B6): RT = 35.9 min (100%) LCMS: m/z = 1309.2 (MH33+). Calculated for (MH33*): 1308.5 Example 20 N-epsilon37-(4-(4-(Tetrazol-5-yl)[1,r,4',1"]terphenyi-4"yloxy)butyroyl)[3-(4-imidazolyl)propionyl7,Aib22,35,Arg26,34lLys37]GLP-1 (7-37) [3-(4-lmidazolyl)propionyl7,Aib22,35,Arg26,34,Lys37]GLP-1 (7-37) peptide was prepared as described in Example 17. The title compound was prepared by acylation of [3-(4- imidazolyl)propionyl7,Aib22,35,Arg26,34,Lys37] GLP-1 (7-37) peptide (18 mg) with (4-(4- (tetrazol-5-yl)[1,1 '.4'.1 "]terphenyl-4"yloxy)butyric acid (8.0 mg) as described for Example 5. 0.83 mg of the title compound was obtained. HPLC: (method B6): RT = 31.9 min (100%) LCMS: m/z = 1303.3 (MH.^). Calculated for(MH3°*): 1303.1 Example 21 N-epsilon37-(2-(2-(2-(16-(Tetrazo!-5-yl)hexadecanoyl)amino)ethoxy)ethoxy)acetyl)[Aib8,22,35,Arg26,34,Lys37] GLP-1 (7-37) The attachment of the linker and sidechain to the specific lysine residue was done on a DDE-Lys(FMOC)-2-CI-Trityl resin by Procedure for removal of the Fmoc-protection, followed by the Procedure for attachment of sidechains to Lysine residues and then the Procedure for removal of Dde-protection. This was followed by synthesis of the peptide to the N-terminus followed by cleavage of the peptide from the resin and purification. HPLC: (method 66i: RT ^ 32.0 min (100%) LCMS: m/z = 1336.2 (MH,!*). Calculated for (MH:/*): 1335.9 Example 22N-epsiion37-(2-(2-(2-(16-(Tetrazoi-5-yl)(hexadecanoylammo)ethoxy)ethoxy)acetyl)) [3-(4-imidazolyl)propionyl7,Aib22,35,Arg26,34,Lys37] GLP-1 (7-37) peptide This compound was prepared as described in example 21. HPLC: (method B6): RT = 32.8 min (99%) LCMS: m/z = 1326.3 (MH33+). Calculated for (MH33t): 1326.2 Example 23 N-epsilon37-(2-(2-(2-(16-(Tetrazol-5yl)hexadecanoyl)amino)ethoxy)ethoxy)acetyl))[3-(4-imidazolyl)propionyl7,Aib8,22,35,Arg26,34,Lys37] GLP-1 (7-37) peptide HPLC: (method B6): RT = 33.0 min (100%) LCMS: m/z = 1330.9 (MH33+). Calculated for (MH33>): 1330.9 Example 24 N-epsilon20-(2-(2-(2-(2-(2-(2-(2-(2-(2-(16-(Tetrazol-5yl)hexadecanoyiamino)ethoxy) ethoxy)acetylamino)ethoxy)ethoxy)acetylamino)ethoxy)ethoxy)acetyl)[Lys20] Exendin-4 (1 -39)amide ; H+B3EGTFTSDLSKCMEEEAVN >i LFI B/VLKNGGPSSGAPPPS«H2 The attachment of sidechains and linkers to specific lysine residues on the crude resin bound protected peptide was carried out in a specific position by incorporation cf Fmoc-Lys(Mtt)-OH during automated synthesis followed by selective deprotection with a batchwise treatment of the protected peptide resin with 1% TFA and 1% TIS in DCM until tne yellow coloring had disappeared (after 1 h). This was followed by extensive wash with DMF, followed by attachment of the spacer and sidechain as described in example 21 and cleavage of the peptide from the resin and purification. HPLC: (method B6): RT = 31.1 min (100%) LCMS: m/z = 1634.3 (MH33*). Calculated for (MH33*): 1634.5 Example 25 (General procedure A, Acylation using human DesBSO insulin) N£BM-(16-?H-Tetrazpl-5-yl-h^^ insulin. Step 1: Synthesis of 2-(16-2H-Tetrazol-5-yl-hexadecanoylamino)pentanedioic acid 1-tert-butyl ester 16-(2H-Tetrazol-5-yl)hexadecanoic acid (433 mg, 1.34 mmol) was heated in toluene (5 ml) and 2,2-dimethoxypropane (2 ml, 16 mmol) to reflux for to minutes. The solvent was removed in vacua, Ethyl acetate (10 ml) was added, followed by /N/-(3-dimethylaminopropyl)-A/'-ethylcarbodiimide hydrochloride (359 mg, 1.87 mmol) and 1 hydroxybenzotriazol (281 mg, 2 mmol). The reaction was stirred at room temperature for 30 min, and a mixture of L- glutamic acid alpha te/f-butyl-gamma benzyl diester hydrochloride (661 mg, 2 mmol), diisopropylamin (0.34 ml, 2 mmol), and ethyl acetate (4 ml) was added. The mixture was stirred at room temperature overnight. The reaction was distributed between ethyl acetate (50 ml) and water (50 ml). The organic phase was dried (Na2S04) and the solvent removed in vacuo. The crude 2-(16-2H-tetrazol-5-yl-hexadecanoylamino)pentanedioic acid 5-benzyl ester 1- ferf-butyl ester was purified on C-18 RP-HPLC 5 cm x 20 cm, flow 20 ml/min using a acetonitriie/water 60-90% gradient containing 0.1% TFA. Fractions containing 2-(16-2H-tetrazol-5-yl-hexadecanoylamino)pentanedioic acid 5-benzyl ester 1- tert-butyl ester were collected and the solvent removed in vacuo. The residue was redissolved in ethyl acetate (10 ml), palladium on activated charcoal (200 mg) was added, and the mixture was stirred under a hydrogen atmosphere (1 atm) for 3 hours. The mixture was filtered and the solvent removed in vacou to yield 2-(16-2H-tetrazol-5-yl-hexadecanoylamino)pentanedioic acid 1-tert-butyl ester (100 mg). HPLC-MS:m/z = 511; R,= 4.17min. Siep_2: Synthesis of 2-(16-2H-Tetrazol-5-yl-hexadecanoylamino)pentanedioic acid 1-tert-butyl ester 5-(2,5-dioxopyrrolidin-1-yl) ester. 2-(16-2H-Tetrazol-5-yl-hexadecanoylamino)-pentanedioic acid 1-tert-butyl ester (100 mg, 0.19 mmol) was dissolved in THF (10 ml). The mixture was cooled with an ice bath. Diisopropylethylamine (0.041 ml, 0.24 mmol) and O-(N-succinimidyl)-N,N,N',N'-tetramethyluronium tetrafluoroborate (71 mg, 0.24 mmol) was added. The mixture was stirred under nitrogen at 0 °C. After 30 minutes the ice cooling was removed and the mixture was stirred for an additional 3 hours. The solvent was removed in vacuo followed by coevaporation of the residue with toluene. The crude product was dissolved in ethyl acetate (30 ml), washed with water (2 y 20 ml), and the combined aqueous phases extracted once with ethyl acetate (30 ml). The combined organic phases were dried (Na2SOJ, the solvent removed in vacuo to yield the title compound (83 mg), which was used in subsequent step without further purification. HPLC-MS: m/z = 607; R,= 4.73 min. Step 3: Synthesis of N[829-(16-2H -Tetrazol-5-yl-hexadecanoyl) gamma-Glu-des(B30) human insulin A1B1BocBoc des(B30) insulin (Kurtzhals P; Havelund S; Jonassen I; Kiehr B: Larsen UD: Ribel U; Markusser, J BiochemicalJournal, 1995, 312, 725-731) (0.2 g, 0.034 mmol) was dissolved in DMSO (3 ml). Triethylamine (0.047 ml, 0.34 mmol) and a solution of 2-(16-2H-tetrazol-5-yl-hexadecanoylamino)pentanedioic acid 1-tert-butyl ester 5-(2,5-dioxo-pyrrolidin-1-yl) ester (58 mg, 0.096 mmol) in DMSO (1mL) were added, and the mixture was shaken at room temperature for 1 hour. The mixture was cooled with an icebath (the DMSO froze), water (10 ml) was added and the frozen mixture was allowed to melt. The pH was adjusted to 5.2 with 1N HCI. The product was allowed to precipitate for 1 hour at 5 °C. The precipitate was isolated by cenirifugation and treated with TFA (10 ml) for 30 min. This solution was poured into ice-cooled diethylether (40 ml), and the crude product was isolated by centrifugation and purified on C-18 RP-HPLC 5 cm x 20 cm, flow 20 ml/min using an acetonitrile/water 25-45% gradient containing 0.1% TFA. Fractions containing the product were combined and lyophilized. To the lyophilized material was added water (7.2 ml) ana the pH adjusted to 8.98 with 1 N and 0.1 N NaOH. The pH was adjusted back to 5.2-5.5 with 0.1 N HCI. The precipitate was isolated by centrifugation and lyophilized to give the title compound. HPLC-MS : m/z = 1536 (m/4), 1229 (m/5),1024 (m/6); R,= 3.47 min. Example 26. NB_25i-4-[4''-(1 H-Te:-azpl-5-yl)-[1,1':4'.1"lterphenyl-4-yloxy]-butyroyl des(B30) insulin 4-(4-(5-TetrazolylH1,1',4',1"]-terphenyl-4"-yloxy)butyric acid (166 mg, 0.42 mmo!) was suspended in DMF (2 ml) and treated with TSTU (150 mg, 0.50 mmol) and DIEA (85 //L, 0.50 mmol). The mixture was stirred overnight. The solvent was removed in vacua and the residue was partitioned between ethyl acetate and 0.1 M HCI. The organic phase/suspension was filtered and the solid was washed with ether and dried in vacua to provide activated 4-(4-(5-tetrazolyl)-[1,1',4',1"]-terphenyl-4"-yloxy)butyric acid, 164 mg. Des(B30) human insulin (100 mg, 0.018 mmol) was dissolved in 100 mM Na2CO3 (1.3 ml, pH 10.2) at room temperature. Activated '4-(4-(5-tetrazolyl)-[1,1',4',1"]-terphenyl-4"-yloxy)butyric acid (10 mg, 0.022 mmol) was dissolved in DMSO (1.3 ml) and added to the insulin solution. After 30 min, 0.2 M methylamine (0.1 ml) was added. pH was adjusted to 5.5 with 1 M HCI, and the isoelectric precipitate was collected by centrifugation and dried in vacua. The coupling yield was 75% ^RP-HPLC, C4 column; buffer A: 10% MeCN in 0.1% TFA-water, buffer B: 30% MeCN in 0.1% TFA-water; gradient 20% to 90% B in 16 minutes). NB2S£-4-[4"-(1H-Tetrazo!-5-yl)[1,r;4',1"]terphenyl-4-yloxy]butyroyl des(B30) insulin was purified by RP-HPLC on C4-column, buffer A: 20% EtOH + 0.1% TFA, buffer B: 80% EtOH + 0.1% TFA; gradient 15-60% B, followed by HPLC on C4-column, buffer A: 10 mM Tris + 15 mM ammonium sulphate in 20% EtOH, pH 7.3, buffer B: 80% EtOH, gradient 15-60% B. The collected fractions were desalted on Sep-Pak with 70% acetonitriie + 0.1% TFA. neutralized by addition of ammonia and freeze-dried. The unoptimized yield was 8 mg (7%). The purity as evaluated by HPLC was >98%. LCMS 6088, C;76H394N6SO77S; requires 6089. Example 27. NB'S£-16-[4'-(1H-tetrazc -5-yl)-biphenyl-4-yloxy]-hexadecanoyl des(B30) insulin 16-(4'-(5-Tetrazolyl)biphenyl-4-yloxy)hexadecanoic acid (309 mg, 0.63 mmol) was suspended in DMF (4 ml) and treated with TSTU (227 mg, 0.75 mmol) and DIEA (127 //L, 0.75 mmol). The mixture was stirred overnight. The solvent was removed in vacua and the residue was partitioned between ethyl acetate and 0.1 M HCI. The organic phase/suspension was filtered and the solid was washed with ether and dried in vacua to provide activated 16-(4'-(5-tetrazoiyl)biphenyl-4-yloxy)hexadecanoic acid, 290 mg. Des(B30) human insulin (100 mg, 0.018 mmol) was dissolved in 100 mM Na2CO3 (1.3 ml, pH 10.2) at room temperature. Activated 1G-(4'-(5-tetrazolyl)biphenyl-4-yloxy)hexadecanoic acid (12 mg, 0.022 mmol) was dissolved in DMSO (1.3 ml) and added to the insulin solution. After 30 min, 0.2 M methylamine (0.1 ml) was added. pH was adjusted to 5.5 with 1 M HCI, and the isoelectric precipitate was collected by centrifugation and dried in vacua. The coupling yield was 37% (RP-HPLC. C4 column: buffer A: 10% MeCN in 0.1% TFA-water, buffer B: 80% MeCN in 0.1% TFA-water; gradient 20% to90% B in 16 minutes). N'1'J'-16-l4'-(1H-Tetrazol-5-yl)biphenyl-4-yloxy]hexadecanoyl des(BSO) insulin was purified by RP-HPLC on C4-column, buffer A: 20% EtOH + 0.1% TFA, buffer B: 80% EtOH + 0.1% TFA; gradient 15-60% B. followed by HPLC on C4-column, buffer A: 10 mM Tris + 15 mM ammonium sulphate in 20% EtOH. pH 7.3, buffer B: 80% EtOH, gradient 15-60% B. The collected fractions were desalted on Sep-Pak with 70% acetonitrile + 0.1% TFA, neutralized by addition of ammonia cind freeze-dried. The unoptimized yield was 5 mg (7%). The purity as evaluated by HPLC was >98%. LCMS 6180, Czj^H^Ng^Sg requires 6181. HPLC-method B4: A: acetonitril B: water D: 1.0% TFA in water Gradient: 5 -> 95% A, 15 min, 1.0 ml/min Symmetry 300, C18. 5//m, 3.9 / 150 mm column Column oven temperature = 42 °C; detection at 214 nm. Example 28. N£37-16-(4-(4-(5-Tetrazolyl)phenyl)phenyloxy)hexadecanoyl)-[Gly8,Arg26,34]GLP-1(7-37) peptide The title compound was prepared as example 6 from 16-(4-(4-(5- tetrazolyl)phenyl)phenyloxy)hexadecanoic acid and [Gly8,Arg26,34]GLP-1-(7-37) peptide (25 mg). 6.1 mg of the title product was obtained. HPLC (method B4): RT = 13.07 min (94%) LCMS: m/z = 1335 (MH33*). Calculated for (MH33+): 1334 Example 29. N'37-(4-(4-(4-(4-(5-Tetrazolyl)phenyl)phenyl)phenoxy)butyryl)[Gly8,Arg26,34]GLP-1-(7-37) peptide The title compound was prepared as example 6 from 4-(4-(4-(4-(5- tetrazolyl)phenyl)phenyl)phenoxy)butyric acid and [Gly8,Arg26,34]GLP-1-(7-37^ peptide (30 mg). 3.8 mg of the title product was obtained. HPLC (method B4): RT = 10.84 min (86%) LCMS: m/z = 1303 (MH33*). Calculated for (MH33t): 1303 Example 30. 17,17-Bis(5-tetrazolyl)beptadecanoic acid 7 7, t 7-Dicyaroheptadezanoic acid methyl ester: To 16-bromcnexadeca-ioip acid methyl ester (1.40 g, 4.0 mmol) in MeCN (20 ml) were added malorodinitrile 1.01 g, 15.3 mmol) and K2C03 (0.92 g, 6.64 mmol). The mixture was stirred at 80 :C for 185 h. Water (50 ml) and 1N HCI (50 ml) were added, and the product was extracted with AcOEt. The combined extracts were washed with brine, dried over MgS04, and concentrated under reduced pressure. 1.87 g (100%) of an oil was obtained which crysta >ized com oletely after some hours. 1H NMR (DN'.SO-d6): C 1.24 (m, 22H), 1.36-1.55 (m, 4H), 1.96 (m, 2H), 2.28 (t, J = 7 Hz, 2H), 3.57 (s,3H). 4.80 (t, v = 7 Hz, 1H). 17,17-Bis(5-:etrazolyi ~eptadecanoic acid methyl ester: To 17,17-dicyanoheptadecanoic acid methyl ester (2.25 g, 6.73 mmol) were added DMF (12 ml), AcOH (4.1 ml, 68 3 mmol), NEt3 (9.0 ml, 64.9 mmol), and NaN3 (5.25 g, 80.8 mmol). The resulting mixture ,vas stirred at 140 °C for 19 h. Water (90 ml) and 1N HCI (60 ml) were added, and the mixture was acidified by addition of concentrated hydrochloric acid. The solid was filtered off, washed with water, and recrystallized from hot methanol, to yield 1.70 g (60%) of the title com round as a solid. 'H NMR (Dr,',SO-d6): ? 1.21 (br s, 24H), 1.51 (m, 2H), 2.19 (m, 2H), 2.28 (t, J = 7 Hz, 2H), 3.57 (s,3H). 4.94 (t. . = 7 Hz, 1H). 17,17-Bis(5-:etrazolyi neptadecanoic acid: 17,17-Bis(5-tetrazolyl)heptadecanoic acid methyl ester (1.70 g, 4.04 mmol) was dissolved in MeOH (40 ml), and a solution of NaOH (1.17 g, 29 mmol) in water (3 ml) was added. After stirring at room temperature for 19 h no more starting ester could be detected by 1H NMR, and the mixture was diluted with a mixture of water (130 ml) and 1N HCI (50 ml). The product was isolated by filtration, washed with water, and recrystallized from boiling MeCN (40 ml), to yield 0.53 g (32%) of the title compound as a solid. From the mother liquor more product (0.39 g) could be obtained. Total yield: 0.92 g, 56%. 1HNMR(DMSO-d6):6 1.21 (m, 24H), 1.48 (m, 2H), 2.18 (m, 4H), 4.94 (t, J = 7 Hz, 1H). Example 31. N£37-(17,17-Bis(5-tetrazolyl)heptadecanoyl)[Gly8,Arg26,34]GLP-1-(7-37)peptide The title compound was prepared as example 6 from 17,17-bis(5-tetrazolyl)heptadecanoic acid and [Gly8,Arg26,34]GLP-l-(7-37) peptide (45 mg). 12.5 mg of the title product was obtained. HPLC (method B4): RT = 11.37 min (91%) LCMS: m/z = 1306 (MH:,3<), 1959 (MH22+). Calculated for (MH33<): 1306 Example 32. 4-(4'..{5-[4-(5-Tetrazolyl)phenyl]-[1,2,4]oxadiazol-3-yl}biphenyl-4-yloxy)butyricacid A mixture of 4'-cyano-4-hydroxybiphenyl (4.0 g, 20.5 mmol), MeCN (30 ml), ethyl 4-bromobutyrate (3.75 ml, 5.11 g, 26.2 mmol), and K2CO3 (3.86 g, 27.9 mmol) was stirred at 85 °C. After 20 h water (150 ml) was added, and the product was extracted with AcOEt. The combined extracts were washed with brine, dried over MgSO4, and concentrated, to yield 6.91 g (100%) of 4-(4'-cyanobiphenyl-4-yloxy)butyric acid ethyl ester as an oil. To a solution of 4-(4'-cyanobiphenyl-4-yloxy)butyric acid ethyl ester (3.78 g, 12.7 mmo!1' in THF (50 ml) was added a solution of NaOH (1.0 g. 25 mmol) in water (1.5 ml). The mixture was stirred at room temperature for 1.5 h and then at 67 °C for 3 h. More NaOH (1 g) in water (1 ml) was added, and stirring at room temperature was contiuned for 15 h. MeOH (10 ml) was added, and after stirring at room temperature for 1.5 h the mixture was diluted with water (150 ml) and acidified with concentrated, aqueous HCI (6.6 ml). The product was isolated by filtration and washed with water (approx 20 ml). The solid was suspended in MeCN (50 ml), heated to reflux (no dissolution) and allowed to cool to room temperature. Filtration and drying under reduced pressure yielded 2.70 g (76%) of 4-(4'-cyanobiphenyl-4-yloxy)butyric acid as a colorless solid. A mixture of 4-(4'-cyanobiphenyl-4-yloxy)butyric acid (2.70 g, 9.60 mmoi), EtOH (10 mi). THF (15 ml), K2CO3 (3.35 g, 24.2 mmol), and hydroxylamine hydrochloride (1.50 g, 21.6 mmol) was stirred at room temperature for 3.5 d, and then at 80 °C for 24 h. Water (100 ml; and 1N HCI (50 ml) were added, and the product was isolated by filtration and washed with water. The solid was suspended in MeCN (70 ml), heated to reflux, kept at room temp overnight, filtratered off, and dried under reduced pressure to yield 3.23 g (100%) of 4-(4'-(N-hydroxycarbamimidoyl)biphenyl-4-yloxy)butyricacid. A solution of 4-cyanobenzoyl chloride (2.29 g, 13.8 mmol) in dioxane (10 ml) was added to a suspension of 4-(4'-(A/-hydroxycarbamimidoyl)biphenyl-4-yloxy)butyric acid (3.23 g, 9.6 mmol) in dioxane (50 ml) and pyridine (2.5 ml, 31.6 mmol). The mixture was stirred at room temperature for 4 h, and then heated to 100 °C for 22 h. The mixture was concentrated to 1/2 of its original volume, diluted with water (100 ml), and acidified by addition of concentrated hydrochloric acid (3 ml). The product was isolated by filtration and washed with water (50 ml). The solid was suspended in MeCN (70 ml), heated to reflux, allowed to cool, filtered off, and dried under reduced pressure to yield 3.17 g (54%) of 4-(4'-{5-[4-cyanophenyl]-[1.2,4]oxadiazol-3-yl}biphenyl-4-yloxy)butyric acid as a solid. A mixture of 4-(4'-{5-[4-cyanophenyl]-[1,2,4]oxadiazol-3-yl}biphenyl-4-yloxy)butyric acid (3.17 g, 7.45 mmol), DMF (15 ml), AcOH (2.25 ml, 37.5 mmol), NEt3 (5.0 ml, 36 mmol), and NaN; (2.89 g. 44.5 mmol) was stirred at 140 °C. After 24 h water (150 ml) and concentrated hydrochloric acid (6 ml) were added. The product was isolated by filtration, washed with water, resuspended in MeCN (100 ml), heated to reflux (it did not dissolve completely), homogenized, and allowed to cool to room temperature. Filtration yielded 2.50 g (72%) of 4-(4'-{5-[4-(5-tetra2olyl)phenyl]-[1,2,4]oxadiazol-3-yl}biphenyl-4-yloxy)butyric acid as a solid. 1H NMR (DMSO-d6): 6 1.98 (m, 2H), 2.41 (t, J = 7 Hz, 2H), 4.06 (t, J = 1 Hz, 2H), 7.07 (d, J = 8 Hz, 2H), 7.72 (d, J = 8 Hz, 2H), 7.88 (d, J = 8 Hz, 2H), 8.16 (d, J = 8 Hz, 2H), 8.32 (d, J = 8 Hz, 2H), 8.41 (d J:=8Hz, 2H). Example 33. N£37-(4-(4'-{5-[4-(5-Tetrazolyl)phenyl]-[1,2,4]oxadiazol-3-yl}biphenyl-4-yloxy)butyryl)[Gly8,Arg26,34]GLP-1-(7-37)peptide The title compound was prepared as example 6 from 4-(4'-{5-[4-(5-tetrazolyl)phenyl]- [1,2,4]oxadiazol-3-yl}biphenyl-4-y!oxy)butyricacid and [Gly8,Arg26,34]GLP-1-(7-37) peptide (60 mg). 1.8 mg of the title product was obtained. HPLC (method B4): RT = 11.26 min (99%) LCMS: m/z = 1326 (MH33*). Calculated for (MH33*): 1326 Example 34 16-(4,5-Bis(5-tetrazolyl)imidazol-1-yl)hexadecanoicacid A mixture of 16-bromohexadecanoic acid methyl ester (3.50 g, 10.02 mmol), 4,5-dicyanoimidazole(1.52g. 12.87 mmol), MeCN (30 ml), and K2CO3(1.95g, 14.1 mmol) was stirred at 80 °C for 66 h. Water (100 ml) and'IN HCI (40 ml) were added, and the product was extracted twice with AcOEt. The combined extracts were washed with brine, dried over MgSO4, and concentrated under reduced pressure. Recrystallization from MeOH (10 ml) yielded 3.41 g (88%) of 16-(4,5-dicyanoimidazol-1-yl)hexadecanoic acid methyl ester as a colorless solid. A mixture of 16-(4,5-dicyanoimidazol-1-yl)hexadecanoic acid methyl ester (3.86 g, 10 mmol), DMF (8 ml), AcOH (6.2 ml, 103 mmol), NEt, (13.8 ml, 100 mmol), and NaN3 (7.98 g. 123 mmol) was stirred at 140 °C. More DMF (9 ml) was added after 20 h. After 44 h water (100 ml) was added, followed by acidification with concentrated hydrochloric acid (approx 12 ml). The product was filtered off, washed with water, resuspended in MeCN (100 ml), heated to reflux (no complete dissolution), and allowed to cool. Filtration and drying under reduced pressure yielded 4.57 g (97%) of 16-(4.5-bis(5-tetrazolyl)imidazol-1-yl)hexadecanoic acid as a brown solid. This solid (4.57 g, 9.67 mmol) was mixed with MeOH (50 ml) and a solution of NaOH (4.01 g, 100 mmol) in water (10 ml). The resulting clear solution was stirred at 60 °C for 22 h, and poured into a stirred mixture of water (400 ml) and concentrated hydrochloric acid (12M, 20 ml). The solid was filtered off, washed with water, resuspended in MeCN (150 ml), heated to reflux, and allowed to stand at room temperature overnight. Filtration and drying under reduced pressure yielded 3.71 g (84%) of the title acid as a brown solid. 1H NMR (DMSO-d6): 6 1.20 (m, 22H), 1.48 (m, 2H), 1.65 (m, 2H), 2.19 (t, J= 7 Hz, 2H), 4.24 (t, J=7Hz, 2H), 8.38(s, 1H). Example 35. Nt37-(16-(4,5-Bis(5-Tetrazolyl)imidazol-1-yl)hexadecanoyl)[Gly8,Arg26,34]GLP-1-(7-37) peptide The title compound was prepared as example 6 from 16-(4,5-bis(5-tetrazolyl)imidazol-1- yl)hexadecanoic acid and [Gly8,Arg26,34]GLP-1-(7-37) peptide (60 mg). 8 mg of the title product was obtained. HPLC (method B4): RT = 11,61 min (98%) LCMS: m/z = 1323 (MH33*). Calculated for (MH,':*): 1323 Example xxx. (2-(2-(16-(5-Tetrazolyl)hexadecanoylamino)elnoxy)ethoxy)acetic acid To a suspension of 2-chlorotrityl chloride resin (2 g; crosslinked polystyrene) in dichloromethane were added a solution of (2-(2-(9H-fluoren-9- ylmethoxycarbonylarnino)ethoxy)ethoxy)acetic acid (0.55 g, 1.43 mmol) in dichloromethane (15 ml) and then a solution of DIPEA (0.65 m!) in dichloromethane (7 ml), After stirring at room temperature for 20 min methanol (2 ml) was added, and stirring was continued for 10 min. The resin was filtered, washed twice with dichloromethane and once with DMF. The resin was treated with a 20%-solution of piperidine in DMF (2x10 min), and washed extensively with DMF and dichloromethane. A solution of 16-(5-tetrazolyl)hexadecanoic acid (1.0 g, 3.08 mmol), 3-hydroxy-3,4-dihydro-1,2,3-benzotriazin-4-one (0.49 g, 3.0 mmol), and EDC (0.58 g, 3.03 mmol) in dichloromethane (25 ml) was added to the resin, and the mixture was shaken for 60 h. The resin was then extensively washed with DMF, dichloromethane and methanol, and suspended in a mixture of trifluoroacetic acid and dichloromethane (25:75; vol). After 0.5 h the resin was filtered, rinsed with dichloromethane, the combined filtrates were concentrated and the residue recrystallized from MeCN to yield 0.26 g of the title compound. 'H NMR (DMSO-d6): 5 1.23(m, 22H), 1.46 (m,2H), 1.67 (m, 2H), 2.04 (t, J = 7 Hz, 2H), 2.85 (t, J = 7 Hz, 2H), 3.18 (m, 2H), 3.38 (m, 2H), 3.51 (m, 2H), 3.58 (m, 2H), 4.01 (s, 2H). Example 36. Nt37-((2-(2-(16-(5-Tetrazolyl)hexadecanoylamino)ethoxy)ethoxy)acetyl) [Gly8,Arg26,34]GLP-1 -(7-37) peptide The title compound was prepared as example 6 from (2-(2-(16-(5- tetrazolyl)hexadecanoylamino)ethoxy)ethoxy)acetic acid and [G!y8,Arg26,34]GLP-1-(7-37) peptide (85 mg). 28 mg of the title product was obtained. HPLC (method 84): RT = 11.35 min (95%) LCMS: m/z = 1327 (MH33*). Calculated for(MH33+): 1327 Example 37. Nt26-(4-{16-(Tetrazol-5-yl)hexadecanoylsulfamoyl}butyryl)[(3-(4-imidazolyl)propionyl7,Arg34]GLP-1-(7-37) peptide This compound was prepared as example 5 from 4-(16-(5- tetrazolyl)hexadecanoylaminosulfonyl)butyric acid acid and [(3-(4- imidazolyl)propionyl7,Arg34]GLP-1-(7-37) peptide (50 mg). 13.3 mg of the title compound was obtained. HPLC (method B4): RT =11.61 min (98%) LCMS: m/z = 1276 (MH33*). Calculated for (MH33+): 1276 Example 38. NEM-(16-{Tetrazol-5-y!}hexadecanoylMGIy8, Arg26] GLP-1 (7-34) peptideamide N The title compound was prepared as example 6 from 16-(5-tetrazolyl)hexadecanoic acid and [Gly8, Arg26] GLP-1 (7-34) peptideamide (50 mg). 17 mg of the title product was obtained. HPLC (method B4): RT = 12.53 min (100%) LCMS: m/z = 1136 (MH;.3t). Calculated for (MH33f): 1136 Example 39. (2-(2-(4-(16-(5-Tetrazolyl)hexadecanoylaminosulfonyl)butyrylamino)ethoxy)ethoxy) acetic acid This compound was prepared on 2-chlorotrityl chloride resin as described for the synthesis of (2-(2-(16-(5-tetrazolyl)hexadecanoylamino)ethoxy)ethoxy)acetic acid. 1H NMR (DMSO-d6): 6 1.23 (m, 22H), 1.49 (m, 2H), 1.68 (m, 2H), 1.85 (m, 2H), 2.23 (m, 4H), 2.85 (t, J = 7 Hz, 2H), 3.19 (m, 2H), 3.35 (m, 4H), 3.52 (m, 2H), 3.59 (m, 2H). 4.01 (s, 2H), 7.91 (brt, J = 6Hz, 1H), 11.55(brs, 1H). Example 40. Ne26-({2-[2-(4-(16-(Tetrazol-5-yl)hexadecanoylsulfamoyl)butyrylamino)ethoxy]ethoxy}acetyl)-[Arg34] GLP-1 (7-37) peptide The title compound was prepared as example 6 from (2-(2-(4-(16-(5-tetrazolyl)hexadecanoylaminosulfonyl)butyrylamino)ethoxy)ethoxy)acetic acid and [Arg34]GLP-1-(7-37) peptide (350 mg). 35 mg of the title product was obtained. HPLC (method B4): RT = 11.63 min (99%) LCMS: m/z = 1329 (MH33+). Calculated for (MH33*): 1329 Example 41. N£34-({2-[2-(4-(16-(Tetrazol-5-yl)hexadecanoylsulfamoyl)butyrylamino)ethoxy]ethoxy}acetyl)- [Arg26] GLP-1 (7-34) peptideamide The title compound was prepared as example 6 from (2-(2-(4-(16-(5-tetrazolyl)hexadecanoylaminosulfonyl)butyrylamino)ethoxy)ethoxy)aceticacid and [Arg26]GLP-1-(7-34) peptide (40 mg). 6.5 mg of the title product was obtained. HPLC (method B4): RT = 12.44 min (100%) LCMS: m/z = 1234 (MH33+). Calculated for (MH33*): 1234 Example 42. N£2b.({2-[2-(4-(16-(Tetrazol-5-yl)hexadecanoylsulfamoyl)butyrylamino)ethoxy]ethoxy}acetyi;-[(3-(4-imidazolyl)propionyl)7,Arg34]GLP-1 (7-37) peptide The title compound was prepared as example 6 from (2-(2-(4-(16-(5- tetrazolyl)hexadecanoylaminosulfonyl)butyrylamino)ethoxy)ethoxy)acetic acid and [ 3-(4- imidazolyl)propionyl)7,Arg34]GLP-1-(7-37) peptide (27 mg). 9.5 mg of the title product was obtained. HPLC (method B4): RT = 11.85 min (96%) LCMS: m/z = 1324 (MH33*). Calculated for (MH33+): 1324 Example 43. N£M-(4-(16-(Tetrazol-5-yt)hexadecanoylsulfamoyl)butyryl)-[Aib8,Arg34]GLP-1-(7-37' peptide The title compound was prepared as example 6 from (4-(16-(5- tetrazolyl)hexadecanoylamino8uJfonyl)butyricacld and [Aib8,Arg34]GLP-1-(7-37) peptide (50 mg). 18.4 mg of the title product was obtained. HPLC (method B4): RT = 11.87 min (95%) LCMS: m/z = 1285 (MH33*). Calculated for (MH33+): 1285 Example 44. Na7(Me)N£26-(4-(16-(Tetrazol-5-yl)hexadecanoylsulfamoyl)butyryl)-[Arg34]GLP-1-(7-37) peptide The title compound was prepared as example 6 from (4-(16-(5- tetrazolyl)hexadecanoylaminosulfonyl)butyricacid and Na7(Me)[Arg34]GLP-1-(7-37) peptide (35 mg). 2.5 mg of the title product was obtained. HPLC (method B4): RT = 11.76 min (96%) LCMS: m/z = 1286 (MH:.3+). Calculated for (MH33*): 1285 Example 45. Nt26-(4-(16-(Tetrazol-5-y!)hexadecanoylsutfamoyl)butyryl)-[Gly8,Arg34]GLP-1-(7-37) peptide The title compound was prepared as example 6 from (4-(16-(5- tetrazolyl)hexadecanoylaminosulfonyl)butyric acid and [Gly8,Arg34]GLP-1-(7-37) peptide (15 mg). 3.2 mg of the title product was obtained. HPLC (method B4): RT = 11.74 min (95%) LCMS: m/z = 1276 (MH33*). Calculated for (MH33+): 1276 Example 46. Nt14-(4-(16-(Tetrazol-5-yl)hexadecanoylsulfamoyl)butyryl)[Lys14;Arg26,34]GLP-1-(7-37) peptide "", The title compound was prepared as example 6 from 4-(16-(5- tetrazolyl)hexadecanoylaminosulfonyl)butyric acid and [Lys14;Arg26,34]GLP-1-(7-37) peptide (65 mg). 19 mg of the title product was obtained. HPLC (method B4): RT =11.54 min (98%) LCMS: m/z = 1304 (MH33+). Calculated for (MH33+): 1304 Compounds which are planned to be synthesised along the procedures described above are Example 47. Nt18-(4-(16-(Tetrazol-5-yl)hexadecanoylsulfamoyl)butyryl)[Lys18;Arg26,34]GLP-1-(7-37) peptide The title compound was prepared as example 6 from 4-(16-(5-tetrazolyl)hexadecanoylaminosulfonyl)butyric acid and [Lys18;Arg26,34]GLP-1-(7-37) peptide (80 mg). 14.5 mg of the title product was obtained. HPLC (method B4): RT = 9.11 min (100%) LCMS: m/z = 1304 (MHa3*). Calculated for (MH3*): 1304 Example 48. N£l8-(4-(16-No.§). 32. A compound according to claim 4, wherein said compound is selected from the group consisting of N-e-26-(1 e-tS-tetrazolylJhexadecanoyiJArg^GLP-l -(7-37), Gly8,Arg26'34GLP-1(7-37)Lys(16-(5-tetrazolyl)hexadecanoyl), Gly8,Arg26'34GLP-1(7-37)Lys{4- [N-(16- [5-tetrazolyl}hexadecanoyl)sulfamoyl]butyryl}, N-e-26-{4-[N-(16-{5- tetrazolyl}hexadecanoyl)sulfamoyl]butyryl} Arg34GLP-1 (7-37), N-£-37-(2-(2-(2-(16-(tetrazol-5-yl)(hexadecanoylamino)ethoxy)ethoxy)acetyl)) Aib8'22'35Lys37GLP-1(7-37), Gly8,Glu22'23'30Arg18-26-34 GLP-1(7-37)Lys(16-(1H-tetrazol-5-yl)hexadecanoic acid [2-(2-{[2-(2- carbamoylmethoxyethoxy)ethylcarbamoyl]methoxy}ethoxy)ethyl]amide)-NH2, and Gly8Arg26'34GLP-1(7-37)Lys(4-(4-(4-(4-(5-tetrazolyl)phenyl)phenyl)phenoxy)butyryl).N-t38-(2- (2-(2-(16-(4-(6-tetrazolyl)phenoxy)hexadecanoyl)ethoxy)ethoxy)acetyl) [Gly8,Arg26,34,Lys38]GLP-1 (7-37) peptide (Figure Remove) J-H GEGTFTSDVSSYLEGQAAREF I AWLVRGR G-N N-epsilon37-(2-(2-(2-( 16-(4-(5- 0 Tetrazolyl)phenoxy)hexadecanoyl)ethoxy)ethoxy)acetyl)[Aib8,22,35,Lys37]GLP-1 (7-37) -N. /r—^(Figure Remove) O H NH2-H-N LJ V J ^>^ " ^JL OH GTFTSDVSSYL E-N,J-Q AAKEF I AWLVK'N ]f-R"N /\ H s-\ H f~H,C CH H.C CH, ° ° Nt38-(2-(2-(2-(16-(Tetrazol-5-yl)hexadecanoyl)ethoxy)ethoxy)acetyl) [Aib8,Arg26,34,Lys38]GLP-1 (7-37) peptide 0 H II NH.-H-N J-L-E GTFTSDVSSYLEGQAAREF I AWLVRGR X H O H3C CH3 Nt38-(4-(N-(16-(Tetrazol-5-yl)hexadecanoyl)sulfamoyl)butyryl)[Aib8,Arg26,34,Lys38]GLP-1(7-37) peptide O ^,- ->" II s ^ A NH H ff H 0 -N^JL-EGTFTSDVSSYL EGQAAREF I AWLV /H3C CH3 N-epsiion32-(4-[N-(16-{5-Tetrazolyl}hexadecanoyl)sulfamoyl]butyryl)-[Lys32]Exendin[1-39] peptide (Figure Remove) GEGTFTSDLSKQMEEEAVRLF I EWL K NGG FNirSG A P P HO HO N-epsilon37-( 1 6-(4 '-(Tetrazol-5-yl)biphenyl)-4-yloxy)hexadecanoyl) imidazolyl)propionyl7,Aib22,35,Arg26,34,Lys37]GLP-1 (7-37) peptide (Figure Remove) N N JJ-E GTFTSDVSSYL E-N )rQ AAREF I AWLV R— N I— R-N T H O A H CH, H3C ^3 O N-epsilon37-( 16-(Tetrazol-5-yl)hexadecanoy I) [3-(4-imidazolyl)propionyl7,Aib22,35,Arg26,34,Lys37]GLP-1 (7-37) (Figure Remove) O H3CyCH3 H O GTFTSDVSSYL E-N\Q AAREF I AWLV R-N J—R N' VOH (Figure Remove) H3C CH3 ° CH, N-epsilon37-( 16-(4-(Tetrazol-5-yl)phenoxy)hexadecanoyl) [3-( imidazolyl)propionyl7,Aib22,35,Arg26,34,Lys37]GLP-1 (7-37) N H3C CH. O 3 V 3 O v H I! X H II VN /-E GTFTSDVSSYLE-N VQ AAREF I AWLV R—N ^P—R-N A " O H3C CH3 n - H " X H N-epsilon37-(4-(4-(Tetrazol-5-yl)[1,1 \4',1 "]terphenyl-4"yloxy)butyroyl) imidazolyl)propionyl7,Aib22,35,Arg26,34,Lys37]GLP-1 (7-37) OH (Figure Remove)HC CH O 3v3 o H || X. H II N /-E GTFTSDVSSYLE-N VQ AAREF I AWLV R—N /—R-N A H o Y H II H H3C CH3 O I CH, N-epsilon37-(2-(2-(2-(16-(Tetrazol-5-yl)hexadecanoyl)amino)ethoxy)ethoxy)acetyl)[Aib8,22,35,Arg26,34,Lys37]GLP-1 (7-37) (Figure Remove) H H NH2-H-N.J1-E GT FTSDVSSYL. E-N "l3(A>x(-'''3 ,-N^U-R-N AAREF I AWLV R N-epsilon37-(2-(2-(2-(16-(Tetrazol-5-yl) (hexadecanoylamino)ethoxy)ethoxy)acetyl))[3-(4-imidazolyl)propionyl7,Aib22,35,Arg26,34,Lys37] GLP-1 (7-37) peptide ,0. ,0 Ht^N O ^V*1' H o GTFI iDVSSYL E-N TrQ AAREF i AWLV R N. J R N' "-» COOH n : H A X H A ° CH, ° H.C'^CH, ° OH N-epsilon37-(2-(2-(2-(16-(Tetrazol-5-yl)hexadecanoyl)amino)ethoxy)ethoxy)acetyl))[3-(4-irnidazolyl)propionyl7tAib8,22,35,Arg26,34,Lys37] GLP-1 (7-37) peptide (Figure Remove)O N-epsilon20-(2-(2-(2-(2-(2-(2-(2-(2-(2-(16-(Tetrazol-5-yl)hexadecanoylamino)ethoxy)ethoxy)acetylamino)ethoxy)ethoxy)acetylamino)ethoxy)ethoxy )acetyl)[Lys20] Exendin-4 (1-39)amide (Figure Remove) H i-NH, "HGEGTFTSDLSKQMEEEAW ]| LFI B/VLKNGGPSSGAPPPS H 0 NtB29-(16-2H-Tetrazol-5-yl-hexadecanoyl) gamma-Glu-des(B30) human insulin, NB29t-4-[4"-(1H-Tetrazol.5-yl)-[1,1';4M"]terphenyl-4-yloxy]-butyroyldes(B30) insulin (Figure Remove) G I V £ Q C C S L Y Q 9TSI LENYC N-COOH FVNQHLC GSHLVEALYLVCOERGFFYT P-H H NB29'--16-[4'-(1 H-tetrazol-5-yl)-biphenyl-4-yloxy]-hexadecanoyl des(B30) insulin (Figure Remove) FVNQHLC GSHLVEALYLVCGERGFFYT P-N Nt37-l6-(4-(4-(5-Tetrazolyl)phenyl)phenyloxy)hexadecanoylHGIy8,Arg26,34]GLP-1-(7-37) peptide Ne37-(4-(4-(4-(4-(5-Tetrazolyl)phenyl)phenyl)phenoxy)butyryl)[Gly8,Arg26,34]GLP-1-(7-37) peptide (Figure Remove) NH,,"H GEGTFTSD . SSYLEGQAA.REF IA -,v I V R G R G N ^ H N£37-(17,17-Bis(5-tetrazolyl)heptadecanoyl)[Giy8,Arg26,34]GLP-1 -(7-37) peptide (Figure Remove) fj H,, — H G t G I f I ;i ; S S > I E . Q A A R Nt3'-(4-(4'-{5-l4-(5-Tetrazolyl)pheny!]-[1,2,4]oxadiazol-3-yl}biphenyl-4-yloxy)butyryl)[Gly8,Arg26,34]GLP-1 -(7-37) peptide (Figure Remove) NH--H & t U 1 f ISC. - S Y I I: G 0' SSYLEGQA A-N H *•.•- H G E G T F (Figure Remove) EFIAWLV^GR G SDVSSYLEGQA A—N H-N >T—E G T H I! 0 H GEGTFTSDVSSYLEGQA A-N EF I AWLVRGR G (Figure Remove) ,—H-N^Tr-E GTFTSDVSSYLEGQ EF I AWLVRGR G NH CT OH H AEGTFTSDVSSYLEGQA A-N' >i E F I AWLVRGR G H (Figure Remove)0 EF I AWLVRGR G —H GEGT FTSDVSSYLEGQA A-N (Figure Remove) (Figure Remove) I > (Figure Remove) m O en O o(Figure Remove) I IZ 73 O O 33 O 33 31 O 33 O —H AEGTFTSDVSSYLEGQA A-N EF I AWLVRGR G—COOH H , „. H H AEGTFTSDVSSYLEGQA A-N >i E f I AWLVRGR G—-OOH H o (Figure Remove) N",— H GEGTFTSDVSSYLEGQA A-N' >i - -E F I AWLVRGR G H O N£2o-(4-(19-(Tetrazol-5-yl)nonadecanoylsulfamoyl)butyryl)[Arg34]GLP-1-(7-37)peptide (Figure Remove)«.-, —H AEGTFTSDVSSYLEGQA A-N' >, E F I AWLVRGR G—=°°» H 0 0 o—9 a 9 a A 1 M V I d 3- 4^ ,N-V V0931ASSAQSldi9 3-4^ ^N-H—*» ,000—0 y 3 M A 1 M V I d 3-—H. N-V V0931ASSAOSidl03V H HN A (Figure Remove) (Figure Remove) —o yOkJAIMV I d 3 U. ,N-V VDO31ASSAaSl.dl030 H (Figure Remove) H AEGTFTSDVSSYLEGQA A-N > E F I AWLVRGR G H 11 0 (Figure Remove) NH H GEGTFTSDVSSYLEGQA A-N >, E F I AWLVRC-R G H 0 (Figure Remove) NH2—H AEGTFTSDVSSYLEGQA A-N' >i E FIAWLVR3R G—coo« H 0 (Figure Remove) NH NH, —H AEGTFTSDVSSYLEGQA A-N' >T E F I AWLVRGR G—COOH H o H GEGTFTSDVSSYLEGQA A-N' > E F I AWLVRGR G—«»H H 0 (Figure Remove) H AEGTFTSDVSSYLEGQA A-N' >i E F I AWLVRGR G—-°°» H 0 NH -HGEGTF"TSDVSSYLEGQA A-N' > E F i AWLVRGR G H 0 NH NH.-H AEGTFTSDVSSYLEGQA A-N' > E F I A W L V R G R O EF I AWLVRGR G—C GTFTSDVSSYLEGQA A-N (Figure Remove)2 H A H AEGTFTSDVSSYt. EGQA A-N H E F I AWLVRGR G (Figure Remove) i,—H AEGTFTSDVSSYLEGQA A-N'^h E F I AWLVRGR G O E GTFTSOVSSY LEGQA A-N^-E FIAWLVRGR G -H-N^E GTFTSDVSSYLEGQA A-N^(Figure Remove)E FIAWLVRGR G H3C CH3 L °OH -^^'0- H •"1-H-M.jL-e G T FTSOVSSY LEGQAAJLJEFIAWLVRG R 0- H,C CM, i ,0^yNH -H--E G T F T S D V S S Y L E G Q A A-E F IA W L V R G R G 33. A compound according to claim 13, wherein the therapeutic a(Figure Remove)gent is human growth hormone or an analog thereof. 34. A compound according to the claim 13, wherein the therapeutic agent is human insulin or an analog thereof. 35. A compound according to claim 13, wherein the therapeutic agent is factor VII or an analog thereof. 36. A compound of the general formula (II) N V_Q_x_Y_z-A-O-R-Lg N-N H (II) wherein G, X, Y, Z. A, Q, and R represent groups as defined in claim 3, and Lg is a leaving group, such as Cl, Br. I, OH, -OS02Me, -OS02CF3, -OTs, -SMe2+, -OSu, -OBt, -OAt, -OPh, or -O(4-NO2)Ph. 37. Use of a compound according to claim 36 for the synthesis of a compound according to any one of claims 4-35. 38. A pharmaceutical composition comprising a compound according to any one of claims 4- 35, and a pharmaceutically acceptable excipient. 39. The pharmaceutical composition according to claim 38, which is suited for parenteral administration. 40. Use of a compound according to any one of the claims 15-32 for the preparation of a medicament for the treatment or prevention of hyperglycemia, type 2 diabetes, impaired glucose tolerance, type 1 diabetes, obesity, hypertension, syndrome X, dyslipidemia, disorders associated with toxic hypervolemia, cognitive disorders, atheroschlerosis, myocardial infarction, coronary heart disease, stroke and other cardiovascular disorders, inflammatory bowel syndrome, dyspepsia and gastric ulcers. 41. Use of a compound according to any one of the claims 15-32 for the preparation of a medicament for delaying or preventing disease progression in type 2 diabetes. 42. Use of a compound according to any one of the claims 15-32 for the preparation of a medicament for decreasing food intake, decreasing (3-cell apoptosis, increasing (3-cell function and ji-celi mass, stimulating p-cell regeneration and/or far restoring glucose sensitivity to (5-cells.