Multifunctional polymer-derivatized γ-Fe2O3 nanocrystals as a methodology for the biomagnetic separation of recombinant His-tagged proteins

M. I. Shukoor; F. Natalio; M. N. Tahir; M. Divekar; N. Metz; H. A. Therese; P. Theato; V. Ksenofontov; H. C. Schröder; W. E.G. Müller; W. Tremel

doi:10.1016/j.jmmm.2008.04.160

Multifunctional polymer-derivatized γ-Fe₂O₃ nanocrystals as a methodology for the biomagnetic separation of recombinant His-tagged proteins

M. I. Shukoor
, F. Natalio
, M. N. Tahir
, M. Divekar
, N. Metz
, H. A. Therese
, P. Theato
, V. Ksenofontov
, H. C. Schröder
, W. E.G. Müller
, W. Tremel^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

Abstract

Multifunctional polymer-derivatized superparamagnetic iron oxide (γ-Fe₂O₃) nanoparticles were prepared for biomagnetic separation of histidine-tagged recombinant proteins building up a faster and efficient method for protein separation by making use of their intrinsic magnetic properties. Using polymer bound γ-Fe₂O₃ nanocrystals, a 6× histidine-tagged recombinant protein (silicatein) with a molecular weight of 24 kDa has been isolated and purified. The supermagnetic iron oxide nanocrystals were characterized by transmission electron microscopy (TEM), high-resolution TEM (HRTEM), SQUID and Mössbauer and the polymer functionalization of the γ-Fe₂O₃ nanocrystals was monitored by UV-vis spectroscopy and light microscopy. Protein immobilization and separation was monitored using immunostaining techniques and gel electrophoresis, respectively.

Original language	English
Pages (from-to)	2339-2344
Number of pages	6
Journal	Journal of Magnetism and Magnetic Materials
Volume	320
Issue number	19
DOIs	https://doi.org/10.1016/j.jmmm.2008.04.160
State	Published - Oct 2008
Externally published	Yes

Bibliographical note

Funding Information:
This research was supported by the Deutsche Forschungsgemeinschaft, the Bundesministerium für Bildung und Forschung, Germany [Center of Excellence BIOTECmarin], the European Society for Marine Biotechnology, the International Human Frontier Science Program, and the Materials Science Center (MWFZ) at the University of Mainz.

Keywords

Maghemite
Multifunctional nanoparticle
Nanoparticle
Protein separation
Silicatein
Surface functionalization

ASJC Scopus subject areas

Electronic, Optical and Magnetic Materials
Condensed Matter Physics

Access to Document

10.1016/j.jmmm.2008.04.160

Cite this

Shukoor, M. I., Natalio, F., Tahir, M. N., Divekar, M., Metz, N., Therese, H. A., Theato, P., Ksenofontov, V., Schröder, H. C., Müller, W. E. G., & Tremel, W. (2008). Multifunctional polymer-derivatized γ-Fe₂O₃ nanocrystals as a methodology for the biomagnetic separation of recombinant His-tagged proteins. Journal of Magnetism and Magnetic Materials, 320(19), 2339-2344. https://doi.org/10.1016/j.jmmm.2008.04.160

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title = "Multifunctional polymer-derivatized γ-Fe2O3 nanocrystals as a methodology for the biomagnetic separation of recombinant His-tagged proteins",

abstract = "Multifunctional polymer-derivatized superparamagnetic iron oxide (γ-Fe2O3) nanoparticles were prepared for biomagnetic separation of histidine-tagged recombinant proteins building up a faster and efficient method for protein separation by making use of their intrinsic magnetic properties. Using polymer bound γ-Fe2O3 nanocrystals, a 6× histidine-tagged recombinant protein (silicatein) with a molecular weight of 24 kDa has been isolated and purified. The supermagnetic iron oxide nanocrystals were characterized by transmission electron microscopy (TEM), high-resolution TEM (HRTEM), SQUID and M{\"o}ssbauer and the polymer functionalization of the γ-Fe2O3 nanocrystals was monitored by UV-vis spectroscopy and light microscopy. Protein immobilization and separation was monitored using immunostaining techniques and gel electrophoresis, respectively.",

keywords = "Maghemite, Multifunctional nanoparticle, Nanoparticle, Protein separation, Silicatein, Surface functionalization",

author = "Shukoor, \{M. I.\} and F. Natalio and Tahir, \{M. N.\} and M. Divekar and N. Metz and Therese, \{H. A.\} and P. Theato and V. Ksenofontov and Schr{\"o}der, \{H. C.\} and M{\"u}ller, \{W. E.G.\} and W. Tremel",

note = "Funding Information: This research was supported by the Deutsche Forschungsgemeinschaft, the Bundesministerium f{\"u}r Bildung und Forschung, Germany [Center of Excellence BIOTECmarin], the European Society for Marine Biotechnology, the International Human Frontier Science Program, and the Materials Science Center (MWFZ) at the University of Mainz.",

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Shukoor, MI, Natalio, F, Tahir, MN, Divekar, M, Metz, N, Therese, HA, Theato, P, Ksenofontov, V, Schröder, HC, Müller, WEG & Tremel, W 2008, 'Multifunctional polymer-derivatized γ-Fe₂O₃ nanocrystals as a methodology for the biomagnetic separation of recombinant His-tagged proteins', Journal of Magnetism and Magnetic Materials, vol. 320, no. 19, pp. 2339-2344. https://doi.org/10.1016/j.jmmm.2008.04.160

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AU - Shukoor, M. I.

AU - Natalio, F.

AU - Tahir, M. N.

AU - Divekar, M.

AU - Metz, N.

AU - Therese, H. A.

AU - Theato, P.

AU - Ksenofontov, V.

AU - Schröder, H. C.

AU - Müller, W. E.G.

AU - Tremel, W.

N1 - Funding Information: This research was supported by the Deutsche Forschungsgemeinschaft, the Bundesministerium für Bildung und Forschung, Germany [Center of Excellence BIOTECmarin], the European Society for Marine Biotechnology, the International Human Frontier Science Program, and the Materials Science Center (MWFZ) at the University of Mainz.

PY - 2008/10

Y1 - 2008/10

N2 - Multifunctional polymer-derivatized superparamagnetic iron oxide (γ-Fe2O3) nanoparticles were prepared for biomagnetic separation of histidine-tagged recombinant proteins building up a faster and efficient method for protein separation by making use of their intrinsic magnetic properties. Using polymer bound γ-Fe2O3 nanocrystals, a 6× histidine-tagged recombinant protein (silicatein) with a molecular weight of 24 kDa has been isolated and purified. The supermagnetic iron oxide nanocrystals were characterized by transmission electron microscopy (TEM), high-resolution TEM (HRTEM), SQUID and Mössbauer and the polymer functionalization of the γ-Fe2O3 nanocrystals was monitored by UV-vis spectroscopy and light microscopy. Protein immobilization and separation was monitored using immunostaining techniques and gel electrophoresis, respectively.

AB - Multifunctional polymer-derivatized superparamagnetic iron oxide (γ-Fe2O3) nanoparticles were prepared for biomagnetic separation of histidine-tagged recombinant proteins building up a faster and efficient method for protein separation by making use of their intrinsic magnetic properties. Using polymer bound γ-Fe2O3 nanocrystals, a 6× histidine-tagged recombinant protein (silicatein) with a molecular weight of 24 kDa has been isolated and purified. The supermagnetic iron oxide nanocrystals were characterized by transmission electron microscopy (TEM), high-resolution TEM (HRTEM), SQUID and Mössbauer and the polymer functionalization of the γ-Fe2O3 nanocrystals was monitored by UV-vis spectroscopy and light microscopy. Protein immobilization and separation was monitored using immunostaining techniques and gel electrophoresis, respectively.

KW - Maghemite

KW - Multifunctional nanoparticle

KW - Nanoparticle

KW - Protein separation

KW - Silicatein

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