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Nano Research 2012, 5(7): 450-459 https://doi.org/10.1007/s12274-012-0230-5
Research Article | Issue | Published: 28 June 2012

Easy Access to Selective Binding and Recyclable Separation of Histidine-Tagged Proteins Using Ni2+-Decorated Superparamagnetic Nanoparticles

Show Author's Information Zhen Liu1,2,  Meng Li1,2,  Zhenhua Li1,2,  Fang Pu1,  Jinsong Ren1( ),  Xiaogang Qu1
State Key Laboratory of Rare Earth Resources Utilization and Laboratory of Chemical Biology Changchun Institute of Applied Chemistry Chinese Academy of SciencesChangchun 130022 China
Graduate School of the Chinese Academy of ScienceBeijing 100039 China
Keywords:
Magnetic nanoparticles, biotechnology, green synthesis, protein purification, recyclable process
Cite this article:
Liu Z, Li M, Li Z, et al. Easy Access to Selective Binding and Recyclable Separation of Histidine-Tagged Proteins Using Ni2+-Decorated Superparamagnetic Nanoparticles. Nano Research, 2012, 5(7): 450-459. https://doi.org/10.1007/s12274-012-0230-5
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Abstract Full text Electronic supplementary material About this article

The development of simple techniques for the separation and purification of recombinant proteins plays an important role in many of the advancements made in biotechnology and nanotechnology. Herein, we report an easy method for the efficient purification of polyhistidine affinity-tagged (His-tagged) proteins by using Ni2+-decorated superparamagnetic particles. Monodisperse Ni0.3Fe0.7Fe2O4 nanoparticles were prepared via a facile and economical one-pot hydrothermal process. Owing to the characteristic molecular recognition ability between nickel(Ⅱ) ions and the polyhistidine affinity tag, the nanoparticles could be successfully employed to selectively bind and separate His-tagged cyan fluorescent protein (CFP) from an E. coli cell lysate in a recyclable process. Moreover, by changing the divalent metal precursors, various other metal-decorated magnetic nanoparticles can be obtained. This approach offers the possibility of constructing metal-decorated nanoparticles through a simple method and will be highly beneficial in further applications of nanoparticle-based technologies.


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Electronic supplementary material
About this article

Easy Access to Selective Binding and Recyclable Separation of Histidine-Tagged Proteins Using Ni2+-Decorated Superparamagnetic Nanoparticles

Show Author's information Zhen Liu1,2, Meng Li1,2, Zhenhua Li1,2, Fang Pu1, Jinsong Ren1( ), Xiaogang Qu1
State Key Laboratory of Rare Earth Resources Utilization and Laboratory of Chemical Biology Changchun Institute of Applied Chemistry Chinese Academy of SciencesChangchun 130022 China
Graduate School of the Chinese Academy of ScienceBeijing 100039 China

Abstract

The development of simple techniques for the separation and purification of recombinant proteins plays an important role in many of the advancements made in biotechnology and nanotechnology. Herein, we report an easy method for the efficient purification of polyhistidine affinity-tagged (His-tagged) proteins by using Ni2+-decorated superparamagnetic particles. Monodisperse Ni0.3Fe0.7Fe2O4 nanoparticles were prepared via a facile and economical one-pot hydrothermal process. Owing to the characteristic molecular recognition ability between nickel(Ⅱ) ions and the polyhistidine affinity tag, the nanoparticles could be successfully employed to selectively bind and separate His-tagged cyan fluorescent protein (CFP) from an E. coli cell lysate in a recyclable process. Moreover, by changing the divalent metal precursors, various other metal-decorated magnetic nanoparticles can be obtained. This approach offers the possibility of constructing metal-decorated nanoparticles through a simple method and will be highly beneficial in further applications of nanoparticle-based technologies.

Keywords: Magnetic nanoparticles, biotechnology, green synthesis, protein purification, recyclable process

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Publication history
Copyright
Acknowledgements

Publication history

Received: 06 April 2012
Revised: 06 May 2012
Accepted: 15 May 2012
Published: 28 June 2012
Issue date: July 2012

Copyright

© Tsinghua University Press and Springer-Verlag Berlin Heidelberg 2012

Acknowledgements

Acknowledgements

Financial support was provided by the National Basic Research Program of China (Grant 2011CB936004) and the National Natural Science Foundation of China (Grants 20331020, 20325101, 20473084, 21072182 and 90913007).

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