title: Trifluoroacetyl tripeptides as potent inhibitors of human leukocyte elastase.
abstract: 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.
mesh_terms: 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
chemical_list: D009842:Oligopeptides; D014269:Trifluoroacetic Acid; D010196:Pancreatic Elastase