An aspartic protease analogue: intermolecular catalysis of peptide hydrolysis by carboxyl groups.
Two aspartic carboxyl groups act as key catalytic groups in the active site of an aspartic protease. We synthesized an aspartic protease analogue by positioning three salicylate residues in close proximity on a cross-linked polystyrene. The immobile artificial protease effectively hydrolyzed albumin into many small fragments by the catalytic action of carboxyl groups contained in the active site. The artificial protease manifested optimum activity at pH 3 just as aspartic proteases.
Oh
S
S
School of Chemistry and Molecular Engineering and Center for Molecular Catalysis, Seoul National University, 151-747, Seoul, Republic of Korea.
Chang
W
W
Suh
J
J
D000418:Albumins / Q000378:metabolism*; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry / Q000378:metabolism; D002384:Catalysis; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D018716:Molecular Mimicry; D010455:Peptides / Q000378:metabolism; D011137:Polystyrenes / Q000737:chemistry*; D012459:Salicylates / Q000737:chemistry*
D000418:Albumins; D010455:Peptides; D011137:Polystyrenes; D012459:Salicylates; D016282:Aspartic Acid Endopeptidases