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 |
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Pages (from-to) | 2339-2344 |
Number of pages | 6 |
Journal | Journal of Magnetism and Magnetic Materials |
Volume | 320 |
Issue number | 19 |
DOIs | |
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