Biologically active analogues of arginine vasopressin containing conformationally restricted dipeptide fragments.
J Pept Res
; 51(2): 149-54, 1998 Feb.
Article
em En
| MEDLINE
| ID: mdl-9516050
ABSTRACT
In this study we described the synthesis and pharmacological properties of five new analogues of arginine vasopressin (AVP). Four of these analogues contained ethylene-bridged dipeptide Phe-Phe in positions 2 and 3; one had two N-Me-Phe residues. All new peptides were tested for vasopressor and antidiuretic activities. We also estimated the uterotonic activities of these compounds in vitro. Three analogues were highly potent V1-antagonists. One of them, namely [Cpa1,(Phe-Phe)2,3,Val4]AVP, which seemed to not interact with either V2 and oxytocic receptors, was outstandingly selective. It is interesting that the high antipressor potency of our second peptide, [(N-Me-Phe)2,3]AVP, was achieved without modification of position 1. Our results open new possibilities for the design of very potent and selective V1-antagonists of AVP.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Conformação Proteica
/
Arginina Vasopressina
/
Dipeptídeos
Limite:
Animals
Idioma:
En
Revista:
J Pept Res
Assunto da revista:
BIOQUIMICA
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
Polônia