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Biomimetic crystallization of MnFe2O4mediated by peptide-catalyzed esterification at low temperature

  • Yoshiaki Maeda
  • , Zengyan Wei
  • , Yasuhiro Ikezoe
  • , Edmund Tam
  • , Hiroshi Matsui*
  • *Corresponding author for this work
  • City University of New York
  • Cornell University

Research output: Contribution to journalArticlepeer-review

Abstract

Enzymes are some of the most efficient catalysts in nature. If small catalytic peptides mimic enzymes, there is potential for broad applications from catalysis for new material synthesis to drug development, due to the ease of molecular design. Recently a hydrogel-based combinatory phage display library was developed and proteasemimicking peptides were identified. Here we advanced the previous discovery to apply one of these catalytic peptides for the synthesis of bimetal oxide nanocrystals through the catalytic ester-elimination pathway. Conventional bimetal oxide crystallization usually requires high temperatures above several hundred 8C; however, this catalytic peptide could grow superparamagnetic MnFe2O4nanocrystals at 48C. Superconducting quantum interference device (SQUID) analysis revealed that MnFe2O4nanocrystals grown by the catalytic peptide exhibit superparamagnetism. This study demonstrates the usefulness of protease-mimicking catalytic peptides in the field of material synthesis.

Original languageEnglish
Pages (from-to)419-422
Number of pages4
JournalChemNanoMat
Volume2
Issue number5
DOIs
StatePublished - 1 May 2016
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

  • Biomineralization
  • Catalytic peptide
  • Ester elimination
  • MnFeO
  • Superparamagnetism

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