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Conformation and activity in angiotensin II peptides
Author(s) -
Fermandjian Serge,
Piriou François,
Sakarellos Constantin,
Lintner Karl,
Khosla Mahesh C.,
Smeby Robert R.,
Bumpus F. Merlin
Publication year - 1981
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1981.360200919
Subject(s) - chemistry , angiotensin ii , circular dichroism , renin–angiotensin system , aqueous solution , oligopeptide , stereochemistry , peptide , biological activity , biophysics , biochemistry , medicine , in vitro , organic chemistry , receptor , blood pressure , biology
Angiotensin II and its competitive inhibitor [Sar 1 , Ile 8 ]‐angiotensin II, as well as several analogs of these two compounds specifically chosen for their well‐defined pharmacological properties, were studied by circular dichroism and nuclear magnetic resonance methods at various pH values in aqueous solution and in d 6 ‐dimethylsulfoxide. The results were compared with their biological activities. This allowed us to establish relationships between conformation and pressor activity, explaining most of the properties of angiotensin II, its inhibitor, and the analogs successively substituted in positions 3 and 5.