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 β-amino acid structure for the potent anti-enzymatic activity.