Premium
Analogs of arginine vasopressin modified in the N ‐terminal part of the molecule with a conformationally constrained cis ‐peptide bond motif
Author(s) -
Sobolewski Dariusz,
Prahl Adam,
Derdowska Izabela,
Slaninová Jiřina,
Kaczmarek Krzysztof,
Zabrocki Janusz,
Lammek Bernard
Publication year - 2007
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.824
Subject(s) - vasopressin , steric effects , arginine , chemistry , uterotonic , peptide , stereochemistry , cyclic peptide , diastereomer , amino acid , biochemistry , endocrinology , biology , oxytocin
The present work is part of our studies aimed at clarifying the influence of steric constraints in the N ‐terminal part of arginine vasopressin (AVP) and its analogs on the pharmacological activity of the resulting peptides. We describe the synthesis of eight new analogs of AVP or [3‐mercaptopropionic acid (Mpa) 1 ]AVP (dAVP) substituted at positions 2 and 3 or 3 and 4 with two diastereomers of 4‐aminopyroglutamic acid. The steric constraints provided by this modification turned out, however, so strong that all the peptides were inactive in all of the bioassays (pressor, antidiuretic and uterotonic tests). Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.