The Effects of N-Terminal Part Modification of Arginine Vasopressin Analogues with 2-Aminoindane-2-carboxylic Acid:  A Highly Potent V2Agonist

2007 ◽  
Vol 50 (12) ◽  
pp. 2926-2929 ◽  
Author(s):  
Wioleta Kowalczyk ◽  
Dariusz Sobolewski ◽  
Adam Prahl ◽  
Izabela Derdowska ◽  
Lenka Borovičková ◽  
...  
Keyword(s):  
Carboxylic Acid ◽  
Arginine Vasopressin ◽  
Terminal Part ◽  
Vasopressin Analogues

Circular dichroism studies of some arginine-vasopressin analogues

1988 ◽  
Vol 31 (1-2) ◽  
pp. 87-100 ◽  
Author(s):  
Zbigniew Grzonka ◽  
Elwira Gwizdała ◽  
Franciszek Kasprzykowski ◽  
Leszek ŁaneKiewicz
Keyword(s):  
Circular Dichroism ◽  
Arginine Vasopressin ◽  
Circular Dichroïsm ◽  
Vasopressin Analogues

Arginine-vasopressin analogues containing D-3-(3′-pyridyl)-alanine residue in position 2

Peptides 1992 ◽  
1993 ◽  
pp. 713-714
Author(s):  
Gotfryd Kupryszewski ◽  
Maria Sobocińska ◽  
Izabela Derdowska ◽  
Jeffrey Schwartz
Keyword(s):  
Arginine Vasopressin ◽  
Alanine Residue ◽  
Vasopressin Analogues

Synthesis and biological properties of vasopressin analogues containing 1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid

1990 ◽  
Vol 55 (4) ◽  
pp. 1099-1105 ◽  
Author(s):  
Zdenko Procházka ◽  
Juris E. Ancans ◽  
Jiřina Slaninová ◽  
Alena Machová ◽  
Tomislav Barth ◽  
...  
Keyword(s):  
Amino Acid ◽  
Carboxylic Acid ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Biological Activities ◽  
Biological Properties ◽  
Phase Synthesis ◽  
Aromatic Residues ◽  
Synthesis Methodology ◽  
Vasopressin Analogues

Solid phase synthesis methodology on a benzhydrylamine resin was used for the synthesis of three analogues of vasopressin with the non-coded amino acid, 1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid (Tic), in the position 2 ([Tic2, Lys8]VP (I)) and in the position 3 ([Tic3, Lys8]VP (II)). The analogue containing only one Tic in place of both aromatic residues was also isolated (des-Tyr2-[Tic3, Lys8]VP (III)). The biological activities of all analogues were negligible.

Analogues of Neurohypophyseal Hormones, Oxytocin and Arginine Vasopressin, Conformationally Restricted in the N-Terminal Part of the Molecule

2006 ◽  
Vol 49 (6) ◽  
pp. 2016-2021 ◽  
Author(s):  
Wioleta Kowalczyk ◽  
Adam Prahl ◽  
Izabela Derdowska ◽  
Dariusz Sobolewski ◽  
Jadwiga Olejnik ◽  
...  
Keyword(s):  
Arginine Vasopressin ◽  
Terminal Part ◽  
Conformationally Restricted ◽  
Neurohypophyseal Hormones

Highly Potent 1-Aminocyclohexane-1-Carboxylic Acid Substituted V2Agonists of Arginine Vasopressin

2004 ◽  
Vol 47 (24) ◽  
pp. 6020-6024 ◽  
Author(s):  
Wioleta Kowalczyk ◽  
Adam Prahl ◽  
Izabela Derdowska ◽  
Olga Dawidowska ◽  
Jiřina Slaninová ◽  
...  
Keyword(s):  
Carboxylic Acid ◽  
Arginine Vasopressin

Analogs of arginine vasopressin modified in theN-terminal part of the molecule with a conformationally constrainedcis-peptide bond motif

2007 ◽  
Vol 13 (2) ◽  
pp. 128-132 ◽  
Author(s):  
Dariusz Sobolewski ◽  
Adam Prahl ◽  
Izabela Derdowska ◽  
Jiřina Slaninová ◽  
Krzysztof Kaczmarek ◽  
...  
Keyword(s):  
Arginine Vasopressin ◽  
Peptide Bond ◽  
Terminal Part

Synthesis, biological activity and receptor binding affinity of two [8-arginine]vasopressin analogues with inhibitory properties

1988 ◽  
Vol 53 (11) ◽  
pp. 2907-2913 ◽  
Author(s):  
Franciszek Kasprzykowski ◽  
Zbigniew Grzonka ◽  
Jiřina Slaninová ◽  
Tomislav Barth ◽  
Peter Crause ◽  
...  
Keyword(s):  
Biological Activity ◽  
Arginine Vasopressin ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Synthesis Method ◽  
The Other ◽  
Binding Affinities ◽  
Bovine Kidney ◽  
Liver Membranes ◽  
Vasopressin Analogues

Two analogues of arginine-vasopressin: [1-(β-mercapto-β,β-cyclopentamethylenepropionic acid), 2-D-phenylalanine, 7-sarcosine, 8-arginine]vasopressin and [1-(β-mercapto-β,β-cyclopentamethylenepropionic acid), 2-D-phenylalanine, 7-N-methylalanine, 8-arginine]vasopressin were synthesized by solid-phase peptide synthesis method. Both peptides exhibit antioxytocic, antivasopressor and antiglycogenolytic activities, and on the other hand they are weak antidiuretic agonists. The binding affinities of both analogues to oxytocic receptor (guinea pig myometrium membranes) and to hepatic V1 receptor (rat liver membranes) are practically the same as for the parent hormones, whereas the binding affinities to renal V2 receptor (bovine kidney membranes) are 60-90 times lower than for vasopressin.

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