title: Inhibition mechanism of trypsin by Schiff base metal chelate inhibitors.
abstract: Studies on trypsin-specific compounds are useful for the design of clinically useful compounds. It is well known that several benzamidine derivatives are potent competitive inhibitors of trypsin and trypsin-like enzymes. Many kinds of Schiff base metal chelate containing either amidine or guanidine have been synthesized and their inhibitory activities against trypsin have been characterized. Recently, the interactions of the Schiff base metal chelate inhibitors with trypsin enzyme have been determined by X-ray crystal structure analysis. The structural information and inhibitory activity data for amidine- and guanidine-containig Schiff base metal chelate inhibitors provide new avenues for designing novel inhibitors against physiologically important trypsin-like serine proteases.
authors: Faculty of Pharmaceutical Sciences, Health Sciences University of Hokkaido, Hokkaido, Japan. iyaguchi@hoku-iryo-u.ac.jp
authors: Daisuke
authors: D
authors: Iyaguchi
mesh_terms: D000578:Amidines; D002614:Chelating Agents / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D018360:Crystallography, X-Ray; D015195:Drug Design; D019791:Guanidine; D008968:Molecular Conformation; D009942:Organometallic Compounds / Q000138:chemical synthesis* / Q000737:chemistry* / Q000494:pharmacology*; D012545:Schiff Bases; D013329:Structure-Activity Relationship; D014361:Trypsin Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*
chemical_list: D000578:Amidines; D002614:Chelating Agents; D009942:Organometallic Compounds; D012545:Schiff Bases; D014361:Trypsin Inhibitors; D019791:Guanidine