journal article·2016-05

Biomimetic Crystallization of MnFe2O4 Mediated by Peptide‐Catalyzed Esterification at Low Temperature

Yoshiaki Maeda, Zengyan Wei, Yasuhiro Ikezoe, Edmund Tam, Hiroshi Matsui

ChemNanoMat· Volume 2· Issue 5
Publisher page

Abstract

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 protease‐mimicking 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 °C; however, this catalytic peptide could grow superparamagnetic MnFe2O4 nanocrystals at 4 °C. Superconducting quantum interference device (SQUID) analysis revealed that MnFe2O4 nanocrystals grown by the catalytic peptide exhibit superparamagnetism. This study demonstrates the usefulness of protease‐mimicking catalytic peptides in the field of material synthesis.
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Research context

OpenAlex topics: Diatoms and Algae Research · Calcium Carbonate Crystallization and Inhibition

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Department of Chemistry and Biochemistry City University of New York—Hunter College 695 Park Ave. New York NY 10065 USA

Department of Biochemistry Weill Medical College of Cornell University 413 E. 69th Street New York NY 10021 USA

Funding

National Institutes of Health (NIH) · Japan Society for the Promotion of Science

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