Synthetic Diversity and Catalytic Mechanism of Peptide Dendrimers
Keywords:Dendrimer, Enzyme model, Ester hydrolysis, Peptide, Solid-phase synthesis
AbstractPeptide dendrimers composed of alternating sequences of natural amino acids and branching diamino acids are investigated as synthetic enzyme models. The dendrimers can be prepared by solid-phase peptide synthesis and are obtained pure in yields of 5–35%. Peptide dendrimers with surface histidine residues catalyze ester hydrolysis reaction with enzyme-like kinetics, including substrate binding (KM), catalytic turnover (kcat), and rate acceleration kcat/kuncat = 1000–20'000. Mechanistic investigation by substrate variation, pH-profile, and isothermaltitration calorimetry show that the catalytic effect is caused by positive interaction between the histidine side-chains and creation of a hydrophobic microenvironment for substrate binding.
How to Cite
E. Delort, T. Darbre, J.-L. Reymond, Chimia 2005, 59, 77, DOI: 10.2533/000942905777676768.
Copyright (c) 2005 Swiss Chemical Society
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