Inhibition of renin by conformationally restricted analogues of angiotensinogen.
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ABSTRACT: [Cys(5),Cys(10)]Angiotensinogen-(5-14)-peptide analogues and homologues were synthesized, in which a disulphide bond between residues 5 and 10 stabilized a 9-->6 beta-turn proposed for the substrate. These compounds were competitive inhibitors of human and pig renins with K(i) values of the order of 10(-6)-10(-5)m, indicating that the conformation proposed for the substrate is important for the interaction with the enzyme.
SUBMITTER: Nakaie CR
PROVIDER: S-EPMC1158444 | biostudies-other | 1982 Jul
REPOSITORIES: biostudies-other
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