title: Symmetrical anhydride-type serine protease inhibitors: structure-activity relationship studies of human chymase inhibitors.
abstract: We prepared a potent and relatively selective human chymase inhibitor 9 (-), based on the study of SAR of a symmetrical anhydride-type serine protease inhibitor 1. Kinetic studies suggested that 9 (-) reacts with the Ser residue at the active site of the enzyme, forming a stable acyl enzyme complex. We also showed the importance of the tri-substituted beta-amino acid structure for the potent anti-enzymatic activity.
authors: Life Science Research Center, Advanced Technology Research Laboratories, Nippon Steel Corporation, Kawasaki, Japan.
authors: K
authors: K
authors: Iijima
authors: J
authors: J
authors: Katada
authors: Y
authors: Y
authors: Hayashi
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D053818:Chymases; D006801:Humans; D007700:Kinetics; D011994:Recombinant Proteins / Q000037:antagonists & inhibitors; D012697:Serine Endopeptidases / Q000187:drug effects*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D013329:Structure-Activity Relationship
chemical_list: D000596:Amino Acids; D011994:Recombinant Proteins; D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases; D053818:Chymases