title: Design of peptide derived amino alcohols as transition-state analog inhibitors of angiotensin converting enzyme.
abstract: A new amino alcohol modification designed to mimic the putative transition-state of amide bond cleavage by proteolytic enzymes has been incorporated into the scissile bond position of N-benzoyl-Phe-Ala-Pro, a known substrate of angiotensin converting enzyme (ACE). The resulting modified tripeptides (i.e. 4) are shown to be a new class of potent inhibitors of converting enzyme.
authors.forename: E M
authors.initials: EM
authors.lastname: Gordon
authors.forename: J D
authors.initials: JD
authors.lastname: Godfrey
authors.forename: J
authors.initials: J
authors.lastname: Pluscec
authors.forename: D
authors.initials: D
authors.lastname: Von Langen
authors.forename: S
authors.initials: S
authors.lastname: Natarajan
mesh_terms: D000605:Amino Alcohols / Q000494:pharmacology*; D000806:Angiotensin-Converting Enzyme Inhibitors; D055598:Chemical Phenomena; D002621:Chemistry; D009842:Oligopeptides / Q000494:pharmacology*; D013329:Structure-Activity Relationship
chemical_list: D000605:Amino Alcohols; D000806:Angiotensin-Converting Enzyme Inhibitors; D009842:Oligopeptides; C029689:benzoylphenylalanyl-alanyl-proline