Synthesis and biological activity of an amino analogue of a tripeptide inhibitor of angiotensin-converting enzyme.
An amino analogue of N-benzoyl-phenylalanyl-glycyl-proline, a tripeptide inhibitor of angiotensin-converting enzyme, was synthesized. The analogue (III) has the phenylalanyl-glycine amide linkage of N-benzoyl-phenylalanyl-glycyl-proline reduced to a methylene amine. Compound III was tested as an inhibitor of porcine plasma angiotensin-converting enzyme and has an I50 of 620 microM compared with an I50 of 9.6 microM for its parent tripeptide. These results are explained in terms of a proposed model of the converting-enzyme active site.
D000806:Angiotensin-Converting Enzyme Inhibitors; D000818:Animals; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D066298:In Vitro Techniques; D007700:Kinetics; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000494:pharmacology; D007703:Peptidyl-Dipeptidase A / Q000097:blood; D013552:Swine
D000806:Angiotensin-Converting Enzyme Inhibitors; D009842:Oligopeptides; C036982:N-benzoylphenylalanyl-glycyl-proline; D007703:Peptidyl-Dipeptidase A