Trifluoroacetyl tripeptides as potent inhibitors of human leukocyte elastase.
Trifluoroacetylated peptides are much more potent inhibitors of human leukocyte elastase than the corresponding unblocked, acylated or benzyloxycarbonylated peptides. The most active compound was trifluoroacetyl-Val-Tyr-Val (Ki = 1.3 micron). A number of free and NH2-terminal-substituted peptides exhibited similar affinities for porcine pancreatic and human leukocyte elastase, indicating that these two enzymes must have similar specificity sites.
D000818:Animals; D001665:Binding Sites; D002151:Calorimetry; D006801:Humans; D007700:Kinetics; D007962:Leukocytes / Q000201:enzymology*; D009842:Oligopeptides / Q000494:pharmacology*; D010179:Pancreas / Q000201:enzymology; D010196:Pancreatic Elastase / Q000097:blood*; D013329:Structure-Activity Relationship; D013552:Swine; D013816:Thermodynamics; D014269:Trifluoroacetic Acid
D009842:Oligopeptides; D014269:Trifluoroacetic Acid; D010196:Pancreatic Elastase