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 p ositioning three salicylate residues in close proximity on a cross-linked p olystyrene. The immobile artificial protease effectively hydrolyzed albumin into many small fragments by the catalytic action of carboxyl groups conta ined in the active site. The artificial protease manifested optimum activit y at pH 3 just as aspartic proteases. (C) 2001 Elsevier Science Ltd. All ri ghts reserved.