Synthesis and Structure-Activity Relationship of Scyliorhinin I Analogues Modified in Position 3, 6, 7 and 8

1993 ◽  
Vol 58 (4) ◽  
pp. 918-924 ◽  
Author(s):  
Jolanta Zboinska ◽  
Krzysztof Rolka ◽  
Gotfryd Kupryszewski ◽  
Krzysztof Golba ◽  
Piotr Imiolek ◽  
...  
Keyword(s):  
Substance P ◽  
Solid Phase ◽  
Phase Method ◽  
Structure Activity ◽  
Dependent Activity ◽  
Solid Phase Method ◽  
Agonistic Activity ◽  
Cd Studies ◽  
Relationship Of ◽  
Dose Dependent

Seven analogues of scyliorhinin I modified in positions 3, 6, 7 and 8 were synthesized by the solid-phase method. Their agonistic activity was determined on isolated guinea pig ileum (GPI). Except for the two analogues modified in position 6, all exhibited dose-dependent activity. Analogues with Phe, D-Phe(F) in position 7 and Abu in position 8 appeared significantly more active than scyliorhinin I and substance P, whereas the analogue with NMeLeu in position 8 appeared to be twice as active as the native molecule, but displayed only 12% of the substance P activity. CD studies indicated that the analogues modified in position 8 behaved differently in the surroundings that mimics the biological membranes.

Antagonistic Analogs of Oxytocin with Substituted Phenylalanine or Tyrosine in Position 2

1994 ◽  
Vol 59 (6) ◽  
pp. 1430-1438 ◽  
Author(s):  
Rudolf Ježek ◽  
Miroslava Žertová ◽  
Jiřina Slaninová ◽  
Pavel Majer ◽  
Zdenko Procházka
Keyword(s):  
Amino Acids ◽  
Solid Phase ◽  
Phase Method ◽  
Inhibiting Activity ◽  
Structure Activity ◽  
Low Degree ◽  
Solid Phase Method ◽  
Pressor Activity ◽  
Agonistic Activity

Solid phase method on p-methylbenzhydrylamine resin was used for the synthesis of seven analogs of oxytocin with non-coded amino acids in position 2. [L-Phe(4-Me)2]oxytocin (I), [D-Phe(4-Me)2]oxytocin (II), [L-Phe(2-Me,4-Et)2]oxytocin (III), [D-Phe(2-Me,4-Et)2]oxytocin (IV), [D-Tyr(Me)2]oxytocin (V), [D-Tyr(Et)2]oxytocin (VI) and [L-Tyr(2-Me)2]oxytocin (VII) were synthesized. All analogs with D-stereoisomer of alkyl or alkoxy substituted phenylalanine possess uterus in vitro inhibiting activity. In the case of L-stereoisomers the structure activity relationship is more complicated. As far as the pressor activity is concerned, the analogs have either very low agonistic activity or low degree of antagonism.

Synthesis and biological activity in GPI test of scyliorhinin I and its analogues modified in position 8 by Leu, Sar and Pro residues

1991 ◽  
Vol 56 (9) ◽  
pp. 1957-1962 ◽  
Author(s):  
Krzysztof Rolka ◽  
Gotfryd Kupryszewski ◽  
Piotr Janas ◽  
Jarosław Myszor ◽  
Zbigniew S. Herman
Keyword(s):  
Biological Activity ◽  
Guinea Pig ◽  
Solid Phase ◽  
Phase Method ◽  
Guinea Pig Ileum ◽  
Tachykinin Receptor ◽  
Solid Phase Method ◽  
One Step ◽  
Agonistic Activity ◽  
The Hill

Three analogues of scyliorhinin I with Gly in position 8 substituted with Leu, Sar and Pro residues, were synthesized by the solid-phase method. The agonistic activity was determined on isolated guinea pig ileum. Analogues with Sar and Pro in position 8 appeared to be significantly more active than scyliorhinin I and the analogues with Leu in this position. For all analogues the Hill cooperativity coefficient is much lower than one suggesting that the interaction of these peptides with tachykinin receptor(s) in not a one-step reaction.

Synthesis of peptides by the solid-phase method. V. Substance P and analogs

1980 ◽  
Vol 58 (4) ◽  
pp. 272-280 ◽  
Author(s):  
A. Fournier ◽  
R. Couture ◽  
J. Magnan ◽  
M. Gendreau ◽  
D. Regoli ◽  
...  
Keyword(s):  
Substance P ◽  
Solid Phase ◽  
Gel Filtration ◽  
Paper Electrophoresis ◽  
Exchange Chromatography ◽  
Phase Method ◽  
Elemental Analyses ◽  
Solid Phase Method

We have synthesized a series of 12 analogs of the undecapeptide substance P in order to perform a structure–activity study of this peptide. In the present work, each residue was substituted by L-alanine, and the C-terminal amide was replaced by the free carboxyl in order to pinpoint biologically important side chains and functional groups. The synthesis of the analogs was carried out by the automatic solid-phase method. Couplings were performed by the symmetrical anhydride procedure. After cleavage with liquid HF, the peptides were purified by gel filtration and ion-exchange chromatography. Their purity was assessed by thin-layer chromatography, paper electrophoresis, amino acid and elemental analyses, and high pressure liquid chromatography. They were tested for biological activity in vitro on the ileum of the guinea pig, the mesenteric vein of the rabbit, and the vas deferens of the rat, and in vivo by measuring their effect on the blood pressure of the rat.

ChemInform Abstract: SYNTHESIS OF PEPTIDES BY THE SOLID-PHASE METHOD. 7. SUBSTANCE P AND ANALOGS

1982 ◽  
Vol 13 (28) ◽  
Author(s):  
A. FOURNIER ◽  
R. COUTURE ◽  
D. REGOLI ◽  
M. GENDREAU ◽  
S. ST-PIERRE
Keyword(s):  
Substance P ◽  
Solid Phase ◽  
Phase Method ◽  
Solid Phase Method

Synthesis of peptides by the solid-phase method. 7. Substance P and analogs

1982 ◽  
Vol 25 (1) ◽  
pp. 64-68 ◽  
Author(s):  
A. Fournier ◽  
R. Couture ◽  
D. Regoli ◽  
M. Gendreau ◽  
S. St-Pierre
Keyword(s):  
Substance P ◽  
Solid Phase ◽  
Phase Method ◽  
Solid Phase Method

Synthesis of peptides by the solid-phase method. IV. Des-Arg9-bradykinin and analogs

1979 ◽  
Vol 57 (8) ◽  
pp. 1084-1089 ◽  
Author(s):  
S. St-Pierre ◽  
P. Gaudreau ◽  
J. N. Drouin ◽  
D. Regoli ◽  
S. Lemaire
Keyword(s):  
Solid Phase ◽  
Gel Filtration ◽  
Rabbit Aorta ◽  
Paper Electrophoresis ◽  
Exchange Chromatography ◽  
Phase Method ◽  
Biological Assays ◽  
Structure Activity ◽  
Solid Phase Method ◽  
First Time

We have synthesized a series of 19 analogs of the octapeptide fragment of bradykinin (BK), des-Arg9-bradykinin, in order to perform a structure–activity study of this peptide on the newly discovered B1 receptor of bradykinin. The first time, each residue of the octapeptide was replaced by L-alanine to pinpoint biologically important residues. Thereafter, both phenylalanine residues in positions 5 and 8 were substituted by L-tyrosine methyl ether, L-cyclohexylalanine, D-phenylalanine, and L-leucine. This paper describes the synthesis of the analogs by the solid phase method. A Beckman peptide synthesizer was used to assemble the peptides on the resin support. Couplings were performed by the symmetrical anhydride procedure. After cleavage with liquid HF, the peptides were purified by ion-exchange chromatography on carboxymethylcellulose and by gel filtration on Bio-Gel P2 resin. The purity of the octapeptides was then checked by tlc, paper electrophoresis, amino acid analysis, and elemental analysis.The new peptides were tested on the rabbit aorta in order to evaluate their kinin-like activities and to see if they act as antagonists. The results of the biological assays are discussed in terms of structure–activity relationships.

Peculiarities of a solid-phase method for the Al-Fe/SiO2 and Al-Co/SiO2 powder catalysts production

2019 ◽  
pp. 63-68
Author(s):  
V.A. Artyukh ◽  
◽  
V.N. Borsch ◽  
V.S. Yusupov ◽  
S.Ya. Zhuk ◽  
...  
Keyword(s):  
Solid Phase ◽  
Phase Method ◽  
Solid Phase Method ◽  
Sio2 Powder

Synthesis and biological activity of new metallocenic angiotensin II analogs

1988 ◽  
Vol 53 (11) ◽  
pp. 2914-2919 ◽  
Author(s):  
Pierrette Maes ◽  
Annie Ricouart ◽  
Emmanuel Escher ◽  
André Tartar ◽  
Christian Sergheraert
Keyword(s):  
Amino Acids ◽  
Biological Activity ◽  
Angiotensin Ii ◽  
Solid Phase ◽  
Rabbit Aorta ◽  
Phase Method ◽  
Solid Phase Method

Analogs of angiotensin II in which phenylalanine in position 8 was replaced with cymantrenylalanine or with its triphenylphosphine photosubstitution product were synthesized by the solid-phase method. On rabbit aorta strips, these peptides were found to be pure antagonists of angiotensin II. Their relative affinities are higher than most other analogs substituted in position 8 with bulky amino-acids.

Synthesis of four new V1 antagonists of arginine-vasopressin (AVP) containing new thioacids at position 1 and their vasoconstrictor activity towards isolated mesenteric arterial vessels of rats

1991 ◽  
Vol 56 (2) ◽  
pp. 491-498 ◽  
Author(s):  
Bernard Lammek ◽  
Izabela Derdowska ◽  
Tomasz M. Wierzba ◽  
Witold Juzwa
Keyword(s):  
Peptide Synthesis ◽  
Arginine Vasopressin ◽  
Solid Phase ◽  
Structural Features ◽  
Phase Method ◽  
Competitive Antagonist ◽  
Vasoconstrictor Effect ◽  
Solid Phase Method

In an attempt to determine some of the structural features in position 1 that account for V1 antagonism, four new analogues of arginine-vasopressin were synthesized and the effect of the modifications on the vasoconstrictor activity was checked using isolated mesenteric arterial vessels of rats. The protected precursors required for these analogues were synthesized by a solid phase method of peptide synthesis. One of the reported analogues, namely [1-(4-mercapto-4-tetrahydrothiopyraneacetic acid)., 2-O-methyltyrosine, 8-arginine]vasopressin appears to be a potent competitive antagonist of the vasoconstrictor effect by AVP.

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