Abstract: A solid pharmaceutical composition for oral administration of small and medium size peptides, particularly vasopressin, oxytocin, and their analogues, comprises said peptide, an enteric coat and a pharmaceutically acceptable carrier containing a buffering agent buffering at a pH of from 2 to 6, preferably at about pH 5. A method of manufacture of single doses of said peptide comprises mixing of the ingredients, forming the resulting mixture into spheres smaller than 2 mm, coating the spheres with an enteric coat which is readily soluble in gastric juice of pH 5.0 or higher but not at substantially lower pH, and filling the coated spheres in capsules or incorporating them into tablets, degradable in the stomach. Also disclosed is a method for oral administration to a patient of said single dose.

Abstract: Disclosed are (1) a DNA containing a cDNA segment coding for human endothelin-2 (SEQ ID NO:1), (2) a precursor of human endothelin-2 (SEQ ID NO:2), (3) a transformant carrying a DNA containing a cDNA segment coding for human endothelin-2, and (4) a method for preparing mature human endothelin-2 which comprises culturing the transformant described in (3), accumulating a protein in a culture medium, and collecting the same, whereby human endothelin-2 and the precursors thereof can be produced in large amounts.

Abstract: A process for preparing and purifying cyclic peptides having disulfide moieties in a single processing operation which simplifies synthesis and reduces production costs, yet produces high, quality yield. Higher yields are obtained by isolating the desired cyclic compound through direct ion exchange chromatography as an integral part of the single process. The improved process is particularly useful for the preparation of vasopressin and oxytocin and their respective derivatives and analogs.

Abstract: Vasopressin analogues of formula (I) ##STR1## wherein X is (S)-2-amino-2-methyl-butanoic acid (CaMeAbu) or Valine (Val), Y is Thienylalanine (Thi) or Methionine (Met), Z is D-Phenylalanine (D-Phe) or D-Thienylalanine (Thi) or D-Tyrosine (D-Tyr), are disclosed. Pharmaceutical preparations comprising a vasopressin analogue of the invention as active ingredient are disclosed and exemplified by oral preparations, nasal preparations, and intravenous preparations. The vasopressin analogues of the invention are intended for use as a medicament, specially an antidiuretic agent. The antidiuretic agent is preferably used for the treatment of diabetes insipidus or enuresis.

Abstract: The invention is directed to the use of a fusion partner that does not contain a leader sequence, as a means to increase the solubility and activity of recombinant polypeptides by facilitating the expression of fusion proteins, which are then transported out of the cytoplasm. The invention includes a nucleic acid encoding a fusion polypeptide comprising a mature interleukin-1-like polypeptide or a leader-deleted-translocating polypeptide, and a polypeptide of interest; as well as host cells comprising such nucleic acids, and fusion proteins so encoded. The invention also encompasses methods of using such nucleic acids to produce recombinant fusion polypeptides, mature polypeptides of interest, and purified compositions thereof.

Abstract: The present invention relates to a novel method for making a predetermined, desired peptide in transgenic animals and can be advantageously used for the production of large quantities of the desired peptide. More particularly, the invention concerns the engineering of a transgenic animal having an artificial gene, which is controlled by globin locus control region (LCR) and which encodes a fusion protein, in which the desired peptide is joined via a cleavable peptide linker to a globin polypeptide. The erythrocytes of the transgenic animal express the fusion globin which is incorporated into hemoglobin produced by the host cell. The desired peptide can be obtained from a hemolysate of the red cells of the transgenic animals by enzymatic or chemical cleavage at the linker.

Abstract: The invention is a class of memory enhancing peptides having the general formula:R.sub.1 --Asn--X.sub.1 --X.sub.2 --X.sub.3 --R.sub.2whereR.sub.1 =pyroglutamyl, acetyl, H, peptidylX.sub.1 =Ala, Ile, Leu, Tyr, Phe, Val, Trp, Cyt, HmeX.sub.2 =Pro, Leu, Ile, Val provided that when X.sub.2 is Pro, X.sub.1 is not Cyt or Ala;X.sub.3 =ArgR.sub.2 =OH, NH.sub.2, OR.sub.3, glycylandR.sub.3 =C.sub.1-6 alkyl.

Abstract: A process for preparing and purifying cyclic peptides having disulfide moieties in a single processing operation which simplifies synthesis and reduces production costs, yet produces high, quality yield. Higher yields are obtained by isolating the desired cyclic compound through direct ion exchange chromatography as an integral part of the single process. The improved process is particularly useful for the preparation of vasopressin and oxytocin and their respective derivatives and analogs.

Abstract: A process for the manufacture of 1-deamino-8-D-arginine vasopressin (DDAVP) comprising, condensing a preparation of Mpa(R.sup.1)-Tyr-Phe-Gln-Asn-Cys(R.sup.2)-Pro-OH (SEQ ID NO: 1), where R.sup.1 and R.sup.2 are sulfhydryl-protecting groups, with the dipeptide (R.sup.3)-D-Arg(HCl)-Gly-NH.sub.2, where R.sup.3 is an acid-sensitive amino-protecting group, to form Mpa(R.sup.1)-Tyr-Phe-Gln-Asn-Cys(R.sup.2)-Pro-D-Arg(HCl)-Gly-NH.sub.2 (SEQ ID NO: 1), which is oxidized with iodine in a protic solvent. The reaction mixture containing the oxidized product can be purified by ion exchange chromatography on a cation exchange resin equilibrated with acid. Also disclosed is high-purity DDAVP obtained by this process and its use for treating diurea.

Abstract: Analogues of 8-D-homoarginine vasopressin were prepared with the general formula ##STR1## where X is L-O-methyltyrosine, L-p-ethylphenylalanine, D-p-ethylphenylalanine, L-p-methylphenylalanine or D-methylphenylalanine and R is cysteine or .beta.-mercaptopropionic acid. These vasopressin analogues exhibited an increased affinity to uterus receptors for oxytocin, where they acted as ocytocin antagonists. Moreover, the analogues of deamino vasopressin have a significantly reduced antidiuretic activity in comparison with [8-D-arginine]vasopressin.

Abstract: Disclosed is a stabilized aqueous composition for administration to a patient comprising a biologically active peptide, a buffer, a quaternary amine-type preservative or disinfectant, and an osmotic pressure-controlling agent, which composition can be stored and used at room temperature. The buffer stabilizes the pH of the composition between about 4 and 6. The preferred buffer contains citrate and/or phosphate, and the preferred preservative or disinfectant is benzalkonium chloride. The composition protects the peptide contained therein from adhering to container surfaces, particularly in containers made of polymeric materials.

Abstract: This invention relates to new vasopressin and vasotocin derivatives of general formula I ##STR1## in which A stands for the radical Mca (=3-mercapto-3,3-cyclpentamethylenepropionyl radical) or for the radical Mpa (=3-mercaptopropionyl radical),B stands for the amino acid radicals D-Tyr, D-Tyr(Et), D-Phe, Tyr(OMe), D-lle, D-Trp, or the radical of a hydrophobic D-amino acid, andC stands for phenylalanine (Phe; vasopressin derivatives) or isoleucine (lle; vasotocin derivatives).They have a high activity toward the oxytocin and the V-vasopressin receptors and can be used for the production of pharmaceutical agents.

Abstract: Disclosed are methods for modelling the three-dimensional structure (tertiary structure) of a ligand having one or more active sites employing a charge-transfer interaction. Also disclosed is a model for Angiotensin II derived from such method.

Abstract: The present invention relates to new vasotocin derivatives with prolonged activity compared to previous vasotocin derivatives. In particular, the vasotocin derivatives of the present invention are of the formula (I) ##STR1## wherein Hmp is a 2-hydroxy-3-mercaptopropionic acid residue, ##STR2## Z is Phe or Tyr, Y is Hgn or Hci, X is a residue of the formula ##STR3## wherein Q is H, alanyl or L-2-aminobutyryl and n is 1, 2 or 3. The present invention also relates to pharmaceutical compositions containing these vasotocin derivatives.

Abstract: Oligopeptides have been found that antagonist cell proliferation stimulated not only by bombesin-like peptides but also other neuropeptides e.g. vasopressin and bradykinin. These oligopeptides block a broad family of mitogenic neuropeptides that bind to receptors that use the inositol signalling pathway and one such receptor has been identified. These oligopeptides are of particular interest in relation to small cell lung cancer.

Abstract: A novel compound is disclosed for inhibiting the effects of oxytocin in a female mammal. As an analog of oxytocin the compound is named [(S)PMP.sup.1,D-Trp.sup.2,Pen.sup.6,Arg.sup.8 ] oxytocin. This compound can be administered to pregnant women to arrest premature labor while avoiding unwanted side effects due to antagonism of the antidiuretic hormone, vasopressin.

Abstract: Electrochemical methods, preferably the Kolbe coupling reaction, are utilized to create intramolecularly bridged peptides, segments or peptide isosteres which are conformationally restricted and preferably, biologically active. Preferably, the peptide analogues contain methylene groups bridging particular amino acid side chains. Analogues of a variety of peptide hormones, including insulin, insulin-like growth factors, somatostatin, melanocyte stimulating hormone, and the like are prepared by the above methods. Such peptides are useful as agonists or antagonists for treatment of diseases associated with deficiency of the hormone or dysregulation of hormone activity, as well as for mechanistic studies to understand the interactions between peptide hormones and cells.

Abstract: Disclosed is a novel peptide having one of the formulae: ##STR1## (A and B are the amino acids: wherein if A is D- or L-Pro, B is Hat or Cit;if A is D-Pro, B is D-Arg, andif B is D- or L-Arg, A is Sat, Pip, Aze or Arg)Asn-A-L- (D-)Pro-Arg- (Gly)n (A is Set, Thr or Ala, n is 1 or 0)A-Ser-Pip-Arg (A is Pro-Asn-, Asn- or Pro-) ##STR2## (A is cyclopentylcarbonyl, Pro or pGlu; B is Gly or .beta.-Ala, W is a hydrogen atom or a group having the formula:or a peptide having the formula: ##STR3## wherein A and B have the same meanings as mentioned above, respectively pGlu-Asn-Ser-A-B-(Gly)n (A is Aze, D- or L-Pro, Pip or Sat, B is D- or L-Arg, Cit, Hat, Lys or Orn, n is 1 or 0) andPro- (Ash)m-Set-L- (D-)Pro-Arg- (Gly) n (m and n are independently 0 or 1)their functional derivatives, and pharmaceutically acceptable salts thereof.

Abstract: Disclosed are cyclic hexapeptides of the formula: ##STR1## These compounds are antagonists of oxytocin and are useful in the treatment of preterm labor and dysmenorrhea, and for stoppage of labor prepatory to Caesarian delivery. Also disclosed are pharmaceutical compositions containing the compounds of formula I and methods of preparing these compounds.

Abstract: A peptide having one of the following formulae (I), (II), (III) and (IV): ##STR1## or its functional derivatives, and a pharmaceutically acceptable salt thereof are disclosed. These peptides have a nootropic effect and are effective as antidementia agents.

Abstract: Cyclic peptides are produced by the controlled aerobic fermentation of Streptomyces silvensis, ATTCC No. 53525 or ATCC No. 53526. These compounds are antagonists of oxytocin and are useful in the treatment of preterm labor and vasopressin and are thus useful in the treatment and prevention of disease states wherein vasopressin may be involved, for example congestive heart failure, hypertension, edema and hyponatremia.

Abstract: A unique class of vasopressin analogue antagonists is provided which have the pharmacological property in-vivo to antagonize pressor (V.sub.1) and/or antidiuretic (V.sub.2) activities. The chemical modifications to the vasopressin 9 member chain sequence at the no. 1, 2, and 4 positions yield a class of potent analogue antagonists which may be employed therapeutically to treat hypertension, congestive heart failure, various edematous situations, and a variety of symptoms due to inappropriate vasopressin secretion.

Abstract: Compounds acting as antagonists of the antidiuretic/and or vasopressor activity of arginine vasopressin are those of the formulaA--CH.sub.2 CO--D--Tyr(R)--Phe--Y--Asn--T--U--Z--Qwherein A is a-adamantyl, cyclohexyl, cyclopentyl, 1-mercaptocyclohexyl, 1-mercaptocyclopentyl, 1-ethyl-1-mercaptopropyl, yclohexylmethyl, cyclopentylmethyl, methyl, isopropyl, tert-butyl or phenyl; R is alkyl of 1-4 carbon atoms; Y is Val, Ile, Thr, Ala, Lys, Cha, Nva, Met, Nle, Orn, Ser, Asn, Gln, Phe, Tyr, Gly, Abu or Leu; T is Pen, Abu, Orn, Oys, Arg, Ala, Cha or Thr; U is Pro, Arg, Lys or Orn or a single bond; Z is (d-or L-) Arg, Orn or Lys and Q is Gly(NH.sub.2), Arg (NH.sub.2), Orn(NH.sub.2), Lys (NH.sub.2), (D- or L-)Ala(NH.sub.2), Ser(NH.sub.2), Val(NH.sub.2), Phe(NH.sub.2), Ile(NH.sub.2), Thr(NH.sub.2), Pro(NH.sub.2), Tyr(NH.sub.2), NH.sub.2, OH, NHR, NGbzl, NH(CH.sub.2).sub.p NH.sub.2 or NH(CH.sub.2).sub.p OH, wherein R is as above and p is an integer from 2 to 6. Compounds wherein T is Cys have similar activity.

Abstract: Novel benzhydrylamine derivatives represented by general formulas (I) and (II) are useful as reaction reagents for the solid-phase synthesis of polypeptide amides making use of 9-fluorenylmethyloxycarbonyl group ("Fmoc"). An intermediate for these derivatives represented by the general formula (III) is also disclosed: ##STR1## where R.sub.1 and R.sub.2 each independently represents a C.sub.1-3 lower alkyl; n is an integer of 1-4; l is 1 or 2; and m is 1 or 2.

Abstract: Composition for the prevention and treatment of autoimmune diseases are provided which comprise as an active ingredient membrane material shed from autoimmune T lymphocytes, or activated T lymphocytes which are treated by a pressure application and releases process. There is also provided processes for obtaining such active materials and for preparing pharmaceutical compositions containing them.

Abstract: Vasopressin-like peptide whose structures have been modified by an alpha-methyl amino acid at the 4 or 7 position are set forth. These compounds have potent vasopressin antagonist activities.

Abstract: Novel analogs of biologically active vasopressin and its synthetic analogs having improved activity are represented by the structural formula: ##STR1## wherein A hydrogen; is hydroxy or lower alkoxy, especially methoxy, B is the peptide residue of phenylalanine (Phe) or isoleucine, Gln represents the peptide residue of glutamine Asn represents the peptide residue of asparagine, E represents the peptide residue of proline (Pro), 4-thioproline (4-thioPro) or 3,4-dehydroproline (3,4-dehydroPro), FNH represents an N-substituted peptide residue of L- or D-lysine (Lys) L or D homolysine (h Lys) or L- or D-orntihine (Orn), X represents a side peptide chain consisting of one or more of Gly, L-Ala, L-Val, L-Leu, or L-Phe, Gly represents the peptide residue of glycine, and G is disulfide (--S--S--) or thioether (--CH.sub.2 S-- or --SCH.sub.2 --).

Abstract: Vasopressin antagonists which have a 4'-methyl-.beta.-mercapto-.beta.,.beta.-cyclopentamethylenepropionic acid group have vasopressin antagonist activity without substantial agonist activity. A species of the invention is [1-(4'-methyl-.beta.-mercapto-.beta.,.beta.-cyclopentamethylenepropionic acid)-2-(O-ethyl)-D-tyrosine-4-valine-8-arginine]vasopressin.

Abstract: The invention concerns novel AVP-binding peptides having the formula:Thr-Met-X-Val-Leu-Thr-Gly-Ser-Pro-Bwherein X is selected from the group consisting of Lys, Arg, and Asp; B is OH, NH.sub.2, NHAlk, wherein Alk is lower alkyl of 1-4 carbons, inclusive. These peptides block AVP function, and, therefore, are useful in many areas among which is the control of hypertension.

Abstract: Compounds acting as antagonists of the antidiuretic/and or vasopressor activity of arginine vasopressin are those of the formula ##STR1## wherein n is 4 or 5; X is (D- or L-)Tyr(R), D-Phe, D-Val, D-Leu, D-Ile, D-Nva, D-Nle, D-Cha, D-Abu, D-Thr, D-Asn, D-Met or D-Gln; Y is Val, Ile, Thr, Ala, Lys, Cha, Nva, Met, Nle, Orn, Ser, Asn, Gln, Phe, Tyr, Gly, Abu or Leu; Z is (D- or L-) Arg, Orn or Lys; Q is Arg(NH.sub.2), Ser(NH.sub.2), (D- or L-)Ala(NH.sub.2), Gly, OH or NH.sub.2 and R is methyl, ethyl, propyl or butyl; provided that, when Y is Gln or Val, R may also be H. Further compounds are those wherein Q is NH(CH.sub.2).sub.3-6 NH.sub.2, NH(CH.sub.2).sub.2-6 OH, NHalk or NHbzl, provided that when Y is Val, Q is other than NHalk or NHbzl. Other compounds are those wherein Q is M-P, wherein M is Gly, (D- or L-)beta-Ala, (D- or L-)Ala, Sar, Orn, Val, Phe, Ile, Thr, Pro, Tyr, Arg or Ser and P is NHalk, NHbzl, NH(CH.sub.2).sub.2-6 OH, NH(CH.sub.2).sub.2-6 NH.sub.

Abstract: Vasopressin antagonists which have a dipeptide tail composed of a neutral and basic amino acid unit demonstrate potent V.sub.1 and V.sub.2 -antagonist activity. Two species of this invention, which are prepared by solid phase peptide synthesis, are [1-(.beta.-mercapto-.beta.,.beta.-cyclopentamethylene propionic acid)-2-(O-ethyl)-D-tyrosine-4-valine-7-tyrosine-8-arginine-9-desglycine]- vasopressin and [1-(.beta.-mercapto-.beta.,.beta.-cyclopentamethylenepropionic acid)-2-(O-ethyl)-D-tyrosine-4-valine-7-arginine-8-tyrosine-9-desglycine]- vasopressin.

Abstract: New compounds which have potent V.sub.2 -vasopressin antagonistic activity are prepared by a 1,6-cyclization using peptide bond formation. The structures of the compounds are characterized by a Pas.sup.1,6 or Tas.sup.1,6 cyclized unit. Also a chiral synthesis of the optically pure Pas intermediates is described.

Abstract: Peptides whose structures resemble those of vasopressin antagonists but have both a carboxamido amino acid unit and a basic amino acid unit in the side chain have good antagonist activity. A species of the invention is [1-(.beta.-mercapto-.beta.,.beta.-cyclopentamethylenepropionic acid)-2-(O-ethyl)-D-tyrosine-4-valine-8-glutamine-9-desglycine]-vasopressi n.

Abstract: Vasopressin antagonists which have a tripeptide side chain comprised of three basic amino acids, such as arginine, lysine or ornithine, demonstrate potent V.sub.1 and V.sub.2 -antagonist activity. A species of the invention, which is prepared by conventional peptide sequencing, is [1-(.beta.-mercapto-.beta.,.beta.-cyclopentamethylenepropionic acid)-2-(O-ethyl)-D-tyrosine-4-valine-7-arginine-8-arginine-9-arginine]-va sopression.

Abstract: Vasopressin antagonists which have a dipeptide side chain comprised of two basic amino acids demonstrate potent V.sub.1 and V.sub.2 -antagonist activity. A species of the invention, which is prepared by conventional peptide sequencing, is [1-(.beta.-mercapto-.beta.,.beta.-cyclopentamethylene propionic acid)-2-(O-ethyl)-D-tyrosine-4-valine-7-arginine-8-arginine-9-desglycine]- vasopressin.

Abstract: Compounds acting as antagonists of the antidiuretic/and or vasopressor activity of arginine vasopressin are those of the formula ##STR1## wherein n is 4 or 5; X is (D- or L-)Tyr(R), D-Phe, D-Val, D-Leu, D-Ile, D-Nva, D-Nle, D-Cha, D-Abu, D-Thr, D-Asn, D-Met or D-Gln; Y is Val, Ile, Thr, Ala, Lys, Cha, Nva, Met, Nle, Orn, Ser, Asn, Gln, Phe, Tyr, Gly, Abu or Leu; Z is (D- or L-) Arg, Orn or Lys; Q is Arg(NH.sub.2), Ser(NH.sub.2), (D- or L-)Ala(NH.sub.2), Gly, OH or NH.sub.2 and R is methyl, ethyl, propyl or butyl; provided that, when Y is Gln or Val, R may also be H.

Abstract: Vasopressin derivatives having unexpected VSP site binding activity whose structures are characterized by a Mpr unit at position 1 and a Pen unit at position 6 are prepared by standard peptide synthetic methods also using an oxidative cyclization of a linear peptide dimercaptan. A representative species is [1-.beta.-mercaptopropionic acid-2-(O-ethyl)-D-tyrosine-4-valine-6-penicillamine-8-arginine]vasopressi n.

Abstract: A peptide with C-terminal proline amide is produced by reacting in aqueous solution a protein substrate having C-terminal prolyl-leucine, prolyl-isoleucine, prolyl-valine, or prolyl-phenylalanine with carboxypeptidase Y in the presence of ammonia. The ammonia is preferably generated by the aqueous reaction of an ammonium salt and an alkali. An example of the peptide product is human calcitonin.

Abstract: Peptides having vasopressin antagonist activity are prepared by a peptide synthesizer to insert a N-methylarginine at the 7-position of the structure. An example of this series of compounds is [1-(.beta.-mercapto-.beta.,.beta.-cyclopentamethylenepropionic acid)-2-(O-ethyl-D-tyrosine)-4-valine-7-desproline-8-N-methylarginine-9-de sglycine]-vasopressin.

Abstract: Certain vasopressin-like peptides, which have an acyclic unit at position 1 and which have an .omega.-amino- or guanidinoalkyl substituent attached to the cysteine in the 6-position of the ring, have V.sub.1 -vasopressin and oxytocin antagonist activity. A species of this series of new compounds is [1-desaminopenicillamine-2-(O-ethyl-D-tyrosine)-8-(1,4-diaminobutane)-9-de sglycinamide]-vasopressin.

Abstract: The preparation of [1-(.beta.-mercapto-.beta.,.beta.-cyclopentamethylenepropionic acid)-2-(O-ethyl-D-tyrosine)-4-valine-8-arginine-9-desglycine]vasopressin by oxidation of the corresponding dimercaptan is improved by using a copper II salt.

Abstract: Compounds acting as antagonists of the antidiuretic/and or vasopressor activity of arginine vasopressin are those of the formula ##STR1## wherein n is 4 or 5; X is (D- or L-)Tyr(R), D-Phe, D-Val, D-Leu, D-lle, D-Nva, D-Nle, D-Cha, D-Abu, D-Thr, D-Asn, D-Met or D-Gln; Y is Val, lle, Thr, Ala, Lys, Cha, Nva, Met, Nle, Orn, Ser, Asn, Gln, Phe, Tyr, Gly, Abu or Leu; Z is (D- or L-) Arg, Orn or Lys; Q is Arg(NH.sub.2), Ser(NH.sub.2), (D- or L-)Ala(NH.sub.2), Gly, OH or NH.sub.2 and R is methyl, ethyl, propyl or butyl; provided that, when Y is Gln or Val, R may also be H. Further compounds are those wherein Q is Orn(NH.sub.2), NHCH.sub.2 CH.sub.2 NH.sub.2, Val(NH.sub.2), Phe(NH.sub.2), lle(NH.sub.2), Thr(NH.sub.2), Pro(NH.sub.2) or Tyr(NH.sub.2).

Abstract: Certain new vasopressin-like peptides which have structures characterized by having a bisaminoalkylbenzene present in the vasopressin tail at the 7- or 8-position retain vasopressin antagonist activity. A species of the invention is [1-.beta.-mercapto-.beta.,.beta.-cyclopentamethylenepropionic acid)-2-(O-ethyl)-D-tyrosine-4-valine-8-1',4'-bis(aminomethyl)benzene-9-de sglycinamide]-vasopressin.

Abstract: Certain vasopressin-like peptides, which have an acyclic unit at position 1 and which have an .omega.-amino- or guanidinoalkyl substituent attached to the cysteine in the 6-position of the ring, have V.sub.1 -vasopressin and oxytocin antagonist activity. A species of this series of new compounds is [1-desaminopenicillamine-2-(O-ethyl-D-tyrosine)-8-(1,4-diaminobutane)-9-de sglycinamide]-vasopressin.

Abstract: Vasopressin derivatives having V.sub.1 and oxytocin antagonist activity whose structures are characterized by a Mpa unit at position 1 and a des-Pro unit at position 7 are prepared by standard peptide synthetic methods also using an oxidative cyclization of a dimercaptan. Representative species are [1-deaminopenicillamine-2-(O-methyl)-tyrosine-7-desproline-8-arginine-9-de sglycine]vasopressin or [1-.beta.-mercaptopropionic acid-2-D-(O-ethyl)tyrosine-3-isoleucine-4-threonine-7-desproline-8-arginin e-9-desglycine]-vasopressin.

Abstract: Modified oxytocin-vasopressin di- or tri-peptides wherein an amide group is replaced by a group selected from ##STR1## --CH.sub.2 NH--, --CH.sub.2 O--, --CH.sub.2 S--, --CH.sub.2 SO--, --CH.sub.2 SO.sub.2 --, --CH.sub.2 CH.sub.2 -- and --CH.dbd.CH-- are described as well as methods for their manufacture, pharmaceutical compositions and methods for treatment, especially of cognitive disorders, depression, morphine dependency and parkinsonism by adjunctive therapy.