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

机译:低温催化肽催化酯化作用的MnFe2O4仿生结晶

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摘要

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.
机译:酶是自然界中一些最有效的催化剂。如果小的催化肽模拟酶,则由于分子设计的简便性,从催化新材料合成到药物开发,都有广泛的应用前景。最近,开发了基于水凝胶的组合噬菌体展示文库,并鉴定了模拟蛋白酶的肽。在这里,我们推进了先前的发现,将这些催化肽之一用于通过催化酯消除途径合成双金属氧化物纳米晶体。传统的双金属氧化物结晶通常需要高于几百摄氏度的高温。然而,这种催化肽可以在4℃下生长超顺磁性MnFe2O4纳米晶体。超导量子干涉装置(SQUID)分析表明,催化肽生长的MnFe2O4纳米晶体具有超顺磁性。这项研究证明了模仿蛋白酶的催化肽在材料合成领域的有用性。

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