Syntheses and Catalytic Actions of Self-Vesicle and Micelle-Forming Enzyme Models of Hydrolase

Abstract

Vesicle-forming catalysts, N- {1- [(3-acety1-4-didodecylcarbamoyl-2-thiazolidinyl) manno-tetra-hydroxybutyl] carbonyl} -L-histidine and-L-histidyl-L-alanine, and micelle-forming catalysts, N- {4- [(3-acetyl-4-dodecylcarbamoyl-2-thiazolidinyl) -manno-tetrahydroxybutyl] carbonyl} -L-his-tidine and-L-histidyl-L-alanine, were designed as hydrolase models. The effects of reaction environment on catalytic activity were examined by the stereoselective hydrolysis of p-nitrophenyl N-ben-zyloxycarbonyl-L- (or D)-phenylalaninate in the absence or presence of cholesterol and/or glycolipids, 3-acetyl-2- (D-manno-pentahydroxypentyl) -4-dodecylcarbamoyl-or-didodecylcarbamoyl-thiazoli-dine. The vesicle-forming catalyst as well as micelle-forming catalyst assisted by vesicle-forming glycolipid showed superior stereorecognition of chiral substrates compared to the micelle-forming catalyst itself. Stereoselectivity increased by the addition of cholesterol. The above findings are discussed in relation to the environment catalysts function.