Inhibition of renin by conformationally restricted analogues of angiotensinogen.
[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.
D000808:Angiotensinogen / Q000378:metabolism / Q000494:pharmacology*; D000809:Angiotensins / Q000494:pharmacology*; D000818:Animals; D002850:Chromatography, Gel; D006801:Humans; D007700:Kinetics; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013552:Swine; D000092502:Renin Inhibitors
D000808:Angiotensinogen; D000809:Angiotensins; D000092502:Renin Inhibitors