Biomimetic Crystallization of MnFe2 O4 Mediated by Peptide-Catalyzed Esterification at Low Temperature
| Autor: | Yoshiaki Maeda, Edmund Tam, Hiroshi Matsui, Yasuhiro Ikezoe, Zengyan Wei |
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| Rok vydání: | 2015 |
| Předmět: |
chemistry.chemical_classification
Materials science Phage display Renewable Energy Sustainability and the Environment Oxide Energy Engineering and Power Technology Peptide Combinatorial chemistry Catalysis Bimetal law.invention Biomaterials chemistry.chemical_compound chemistry Nanocrystal Biocatalysis law Materials Chemistry Crystallization |
| Zdroj: | ChemNanoMat. 2:419-422 |
| ISSN: | 2199-692X |
| DOI: | 10.1002/cnma.201500181 |
| Popis: | 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 nano-crystals grown by the catalytic peptide exhibit superpara-magnetism. This study demonstrates the usefulness of protease-mimicking catalytic peptides in the field of material synthesis. |
| Databáze: | OpenAIRE |
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