Influence of Conformationally Constrained Amino Acids Replacing Positions 2 and 3 of Arginine Vasopressin (AVP) and Its Analogues on Their Pharmacological Properties

Title: Influence of Conformationally Constrained Amino Acids Replacing Positions 2 and 3 of Arginine Vasopressin (AVP) and Its Analogues on Their Pharmacological Properties

Volume: 14 Issue: 3

Author(s): Dariusz Sobolewski, Adam Prahl, Izabela Derdowska, Anna Kwiatkowska, Jirina Slaninova and Bernard Lammek

Affiliation:

Keywords: Analogues of arginine vasopressin (AVP), 4-aminobenzoic acid (Abz), cis-4-aminocyclohexanecarboxylic acid(ach), trans-4-aminocyclohexanecarboxylic acid (Ach), biological activity

Abstract: Synthesis of thirteen new analogues of arginine vasopressin (AVP) has been described. Amino acid residues at positions 2 and 3 of AVP, [3-mercaptopropionic acid (Mpa)1]AVP (dAVP), [Mpa1,D-Arg8]VP (dDAVP) and [Mpa1,Val4,D-Arg8]VP (dVDAVP) were replaced with one amino acid residue using sterically constrained nonproteinogenic amino acids, 4-aminobenzoic acid (Abz), cis-4-aminocyclohexanecarboxylic acid (ach) or its trans-isomer (Ach). In the case of a potent V1a antagonist, [1-mercaptocyclohexaneacetic acid (Cpa)1]AVP, only one similar analogue has been prepared by replacing positions 2 and 3 with Abz. Unfortunately, all new peptides were inactive in bioassays for the pressor, antidiuretic and uterotonic in vitro activities in the rat.

Cite this article as:

Sobolewski Dariusz, Prahl Adam, Derdowska Izabela, Kwiatkowska Anna, Slaninova Jirina and Lammek Bernard, Influence of Conformationally Constrained Amino Acids Replacing Positions 2 and 3 of Arginine Vasopressin (AVP) and Its Analogues on Their Pharmacological Properties, Protein & Peptide Letters 2007; 14 (3) . https://dx.doi.org/10.2174/092986607780090810