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Analogs of arginine vasopressin modified in the N-terminal part of the molecule with a conformationally constrained cis-peptide bond motif

✍ Scribed by Dariusz Sobolewski; Adam Prahl; Izabela Derdowska; Jiřina Slaninová; Krzysztof Kaczmarek; Janusz Zabrocki; Bernard Lammek

Book ID
105360647
Publisher
John Wiley and Sons
Year
2007
Tongue
English
Weight
124 KB
Volume
13
Category
Article
ISSN
1075-2617

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✦ Synopsis

Abstract

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.

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✍ Dariusz Sobolewski; Adam Prahl; Anna Kwiatkowska; Jiřina Slaninová; Bernard Lamm 📂 Article 📅 2009 🏛 John Wiley and Sons 🌐 English ⚖ 121 KB

## Abstract Using SPPS techniques, six new analogues of AVP and some of its agonists were synthesised. The peptides were designed by substitution of Phe at position 3 of AVP, [Mpa^1^] AVP (dAVP) and [Mpa^1^,Val^4^,D‐Arg^8^]VP (dVDAVP) with L‐ or D‐Pip, a non‐coded α‐imino acid, also called homoprol