Synthetic Diversity and Catalytic Mechanism of Peptide Dendrimers

Authors

  • Estelle Delort
  • Tamis Darbre
  • Jean-Louis Reymond

DOI:

https://doi.org/10.2533/000942905777676768

Keywords:

Dendrimer, Enzyme model, Ester hydrolysis, Peptide, Solid-phase synthesis

Abstract

Peptide 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.

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Published

2005-03-01

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