Hydrolytic reaction catalyzed by poly[N-(substituted)glycine]s having imidazolyl groups in side chains in the presence of liposome.
Hydrolytic reactions in the presence of liposomes catalyzed by N epsilon-benzyloxycarbonylhistidine groups introduced into the side chains of poly[N-(3-aminopropyl)glycine] were studied. On increasing the hydrophobicity of the polypeptide catalyst by introducing dodecyl groups into the side chains, and in the presence of dipalmitoylphosphatidylcholine (DPPC) bilayer membranes, p-nitrophenyl palmitate (PNPP) was hydrolyzed more rapidly than p-nitrophenyl acetate (PNPA). The addition of cholesterol or phosphatidylserine to lipid bilayer membranes accelerated the hydrolysis of PNPP catalyzed by the polypeptide catalyst more strongly than that of PNPA. The substrate selectivity and catalytic efficiency of the polypeptide catalyst were found to be controlled by the physical state of the lipid bilayer membranes.
Yagi
Y
Y
Department of Polymer Chemistry, Kyoto University, Japan.
Kimura
S
S
Imanishi
Y
Y
D015060:1,2-Dipalmitoylphosphatidylcholine; D002384:Catalysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002784:Cholesterol / Q000494:pharmacology; D006868:Hydrolysis; D007093:Imidazoles; D008051:Lipid Bilayers; D008081:Liposomes; D009596:Nitrophenols; D010168:Palmitates; D010169:Palmitic Acids; D010455:Peptides; D010718:Phosphatidylserines / Q000494:pharmacology; D011108:Polymers; D011437:Propylamines
D007093:Imidazoles; D008051:Lipid Bilayers; D008081:Liposomes; D009596:Nitrophenols; D010168:Palmitates; D010169:Palmitic Acids; D010455:Peptides; D010718:Phosphatidylserines; D011108:Polymers; D011437:Propylamines; C062553:poly(N-(3-aminopropyl)glycine); C050015:4-nitrophenyl palmitate; D015060:1,2-Dipalmitoylphosphatidylcholine; C008642:4-nitrophenyl acetate; D002784:Cholesterol