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Enzyme-Mimicking Peptides to Catalytically Grow ZnO Nanocrystals in Non-Aqueous Environments

  • Yoshiaki Maeda
  • , Zengyan Wei
  • , Yasuhiro Ikezoe
  • , Hiroshi Matsui*
  • *Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

The application of enzymes for biomimetic material growth is a potential path to breakthroughs in catalytic inorganic nanocrystal synthesis because the biocatalytic functions of proteins can lead to highly efficient growth of materials with accurate structures at low temperature. However, many metal nanocrystals are grown in organic solvents, which is not an ideal environment for biomineralization with enzymes due to denaturing of catalytic pocket structures. Here, we applied a catalytic CP4 peptide, optimized for protease reactions such as amide and ester hydrolysis, to test the catalytic ZnO nanocrystal growth in non-aqueous environments and the performance was compared with the enzyme subtilisin. We demonstrated that the CP4 catalytic peptide, evolved by the hydrogel-based combinatory phage display library, could grow ZnO nanoparticles from zinc acetate precursors in higher crystallinity and yield, as compared to the protease enzyme, in an organic solvent by catalyzing ester-elimination of precursors at room temperature. This result indicates that catalytic oligopeptides, which possess no rigid 3D structures but are rather flexible, could fold into the catalytically active conformation more frequently in harsh environments such as organic solvents.

Original languageEnglish
Pages (from-to)319-323
Number of pages5
JournalChemNanoMat
Volume1
Issue number5
DOIs
StatePublished - Sep 2015
Externally publishedYes

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

  1. SDG 7 - Affordable and Clean Energy
    SDG 7 Affordable and Clean Energy

Keywords

  • biocatalysis
  • biomimetics
  • biomineralization
  • peptides
  • phage library

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