Inhibition of renin by conformationally restricted analogues of angiotensinogen

Abstract

[Cys5,Cys10]Angiotensinogen-(5–14)-peptide analogues and homologues were synthesized, in which a disulphide bond between residues 5 and 10 stabilized a 9→6 β-turn proposed for the substrate. These compounds were competitive inhibitors of human and pig renins with Ki values of the order of 10−6–10−5m, indicating that the conformation proposed for the substrate is important for the interaction with the enzyme.