Catalytic peptide dendrimers

Abstract

Enzymelike kinetics were observed in the hydrolysis of 7-hydroxy-1-methylquinolium esters 2 under the catalysis of three of a family of synthetic peptide dendrimers 1. Their synthesis was based on a symmetrical branching diamino acid (B), three variable amino acid positions (A1, A2, A3 = His, Asp, Ser), and a disulfide bond dimerization strategy. All possible permutations of the catalytic triad of the amino acids aspartate, histidine, and serine at the variable positions gave a family of 21 peptide dendrimers.