Influence of Conformationally Constrained Amino Acids Replacing Positions 2 and 3 of Arginine Vasopressin (AVP) and Its Analogues on Their Pharmacological Properties
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.
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Document Type: Research Article
Affiliations: Faculty of Chemistry, University of Gda sk, Sobieskiego 18, 80-952 Gda sk, Poland.
Publication date: 2007-03-01
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