One-pot synthesis of CuFe2O4 magnetic nanocrystal clusters for highly specific separation of histidine-rich proteins

One-pot synthesis of CuFe2O4 magnetic nanocrystal clusters for highly specific separation of histidine-rich proteins
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一锅合成 CuFe2O4 磁性纳米晶簇,用于高度特异性分离富含组氨酸的蛋白质

DOI:
10.1039/c4tb00986j
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发表时间:
2014
期刊:
J. Mater. Chem. B
影响因子:
--
通讯作者:
Lan Zhang
Lan Zhang
中科院分区:
其他
文献类型:
--
作者:
Jiangnan Zheng;Zian Lin;Wei Liu;Ling Wang;Sen Zhao;Huanghao Yang;Lan Zhang

文献摘要

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这项工作报告了一种简便的无配体方法,可使用 CuFe2O4 磁性纳米晶体簇 (MNC) 快速、高度特异性地分离富含组氨酸 (His) 的蛋白质。通过简单且经济的一锅水热法合成了单分散的 CuFe2O4 MNCs。由此产生的跨国公司被详细描述。测量结果表明,MNCs表现出良好的分散性、高结晶度和超顺磁性。此外,所获得的MNC具有高饱和磁化强度(45.1 emu g−1),足以在外部磁场下实现快速有效的分离。使用富含 His 的蛋白质(牛血红蛋白)和含有较少表面暴露 His 残基的其他蛋白质(牛血清白蛋白、人血清白蛋白、肌红蛋白、溶菌酶、细胞色素 c 和辣根过氧化物酶)作为模型样品,评估 CuFe2O4 MNC 的选择性和结合能力。 CuFe2O4 MNCs 最显着的特征是由于铜(II)离子和血红蛋白表面暴露的组氨酸残基之间的配位而具有高血红蛋白结合能力(4475 mg g−1)。此外,CuFe2O4 MNC 可以成功地用于选择性结合和去除人体血液样本中丰富的血红蛋白。良好的结果证明了 CuFe2O4 MNC 在分离富含 His 的蛋白质方面的潜力。
This work reports a facile ligand-free method for the rapid and highly specific separation of histidine (His)-rich proteins using CuFe2O4 magnetic nanocrystal clusters (MNCs). Monodispersed CuFe2O4 MNCs were synthesized via a simple and economical one-pot hydrothermal process. The resulting MNCs were characterized in detail. The measurements indicated that the MNCs exhibited good dispersion, high crystallinity, and superparamagnetic properties. Moreover, the obtained MNCs had a high saturation magnetization (45.1 emu g−1), which was sufficient to accomplish fast and efficient separation with an external magnetic field. The selectivity and binding capacity of CuFe2O4 MNCs were evaluated using a His-rich protein (bovine haemoglobin) and other proteins (bovine serum albumin, human serum albumin, myoglobin, lysozyme, cytochrome c and horseradish peroxidase) containing fewer surface-exposed His residues as model samples. The most distinct feature of the CuFe2O4 MNCs is the high haemoglobin binding capacity (4475 mg g−1) due to the coordination between copper(II) ions and surface-exposed histidine resides of haemoglobin. In addition, the CuFe2O4 MNCs can be successfully employed to selectively bind and remove abundant haemoglobin from human blood samples. The good results demonstrate the potential of CuFe2O4 MNCs in the separation of His-rich proteins.