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Analogues of arginine vasopressin modified in position 2 and 3 with conformationally constrained dipeptide fragments

✍ Scribed by Elżbieta Łempicka; Izabela Derdowska; Wioleta Kowalczyk; Olga Dawidowska; Adam Prahl; Marcin Janecki; Tomasz Jasiński; Henryk I. Trzeciak; Bernard Lammek

Book ID
111701218
Publisher
John Wiley and Sons
Year
2005
Tongue
English
Weight
103 KB
Volume
11
Category
Article
ISSN
1075-2617

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📜 SIMILAR VOLUMES

An investigation of position 3 in argini
An investigation of position 3 in arginine vasopressin with aliphatic, aromatic, conformationally-restricted, polar and charged amino acids
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We report the solid-phase synthesis and some pharmacological properties of 23 new analogs of arginine vasopressin (AVP) which have the Phe 3 residue replaced by a broad variety of amino acids. Peptides 1 -9 have at position 3: (1) the mixed aromatic/aliphatic amino acid thienylalanine (Thi) and the

Analogs of arginine vasopressin modified
Analogs of arginine vasopressin modified in the N-terminal part of the molecule with a conformationally constrained cis-peptide bond motif
✍ Dariusz Sobolewski; Adam Prahl; Izabela Derdowska; Jiřina Slaninová; Krzysztof K 📂 Article 📅 2007 🏛 John Wiley and Sons 🌐 English ⚖ 124 KB

## 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