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 language | English |
|---|---|
| Pages (from-to) | 419-422 |
| Number of pages | 4 |
| Journal | ChemNanoMat |
| Volume | 2 |
| Issue number | 5 |
| DOIs | |
| State | Published - 1 May 2016 |
| Externally published | Yes |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 7 Affordable and Clean Energy
Keywords
- Biomineralization
- Catalytic peptide
- Ester elimination
- MnFeO
- Superparamagnetism
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