Issue 38, 2013

Ferroferric oxide/l-cysteine magnetic nanospheres for capturing histidine-tagged proteins

Abstract

Ferroferric oxide/L-cysteine (Fe3O4/Cys) nanospheres (NSs) have been successfully synthesized via a facile solvothermal route. Fe3O4/Cys NSs possessed high thiol group density and saturation magnetization (Ms) of 84.6 emu g−1. The prepared magnetic NSs are biocompatible and manipulatable by an external magnetic force. After chelating Ni2+ ions, Fe3O4/Cys-Ni2+ NSs were used to enrich and purify histidine-tagged (His-tagged) proteins directly from the mixture of lysed cells without pretreatment. It has been found that Fe3O4/Cys-Ni2+ NSs present negligible nonspecific protein adsorption and high protein binding activity with the saturation capacity being 53.2 μg mg−1 and they are especially suitable for rapid purification of His-tagged proteins.

Graphical abstract: Ferroferric oxide/l-cysteine magnetic nanospheres for capturing histidine-tagged proteins

Supplementary files

Article information

Article type
Paper
Submitted
22 May 2013
Accepted
24 Jul 2013
First published
25 Jul 2013

J. Mater. Chem. B, 2013,1, 5108-5113

Ferroferric oxide/L-cysteine magnetic nanospheres for capturing histidine-tagged proteins

X. Zou, K. Li, Y. Zhao, Y. Zhang, B. Li and C. Song, J. Mater. Chem. B, 2013, 1, 5108 DOI: 10.1039/C3TB20726A

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