Design of peptide derived amino alcohols as transition-state analog inhibitors of angiotensin converting enzyme.
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.
Gordon
E M
EM
Godfrey
J D
JD
Pluscec
J
J
Von Langen
D
D
Natarajan
S
S
D000605:Amino Alcohols / Q000494:pharmacology*; D000806:Angiotensin-Converting Enzyme Inhibitors; D055598:Chemical Phenomena; D002621:Chemistry; D009842:Oligopeptides / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D000605:Amino Alcohols; D000806:Angiotensin-Converting Enzyme Inhibitors; D009842:Oligopeptides; C029689:benzoylphenylalanyl-alanyl-proline