Self-Assembled Peptide Nano-Superstructure towards Enzyme Mimicking Hydrolysis

Angew Chem Int Ed Engl. 2021 Jul 26;60(31):17164-17170. doi: 10.1002/anie.202105830. Epub 2021 Jun 24.

Abstract

The structural arrangement of amino acid residues in native enzymes underlies their remarkable catalytic properties, thus providing a notable point of reference for designing potent yet simple biomimetic catalysts. Herein, we describe a minimalistic approach to construct a dipeptide-based nano-superstructure with enzyme-like activity. The self-assembled biocatalyst comprises one peptide as a single building block, readily synthesized from histidine. Through coordination with zinc ion, the peptide self-assembly procedure allows the formation of supramolecular β-sheet ordered nanocrystals, which can be used as basic units to further construct higher-order superstructure. As a result, remarkable hydrolysis activity and enduring stability are demonstrated. Our work exemplifies the use of a bioinspired supramolecular assembly approach to develop next-generation biocatalysts for biotechnological applications.

Keywords: biocatalysis; nano-superstructure; peptide; self-assembly; supramolecular chemistry.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Histidine / chemistry
  • Hydrolysis
  • Nanoparticles / chemistry*
  • Particle Size
  • Peptides / chemical synthesis
  • Peptides / chemistry*

Substances

  • Peptides
  • Histidine