[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.