| Literature DB >> 18400567 |
Marjan Bele1, Gorazd Hribar, Stanislav Campelj, Darko Makovec, Vladka Gaberc-Porekar, Milena Zorko, Miran Gaberscek, Janko Jamnik, Peter Venturini.
Abstract
The aim of this study was to be able to reversibly bind histidine-rich proteins to the surface of maghemite magnetic nanoparticles via coordinative bonding using Zn ions as the anchoring points. We showed that in order to adsorb Zn ions on the maghemite, the surface of the latter needs to be modified. As silica is known to strongly adsorb zinc ions, we chose to modify the maghemite nanoparticles with a nanometre-thick silica layer. This layer appeared to be thin enough for the maghemite nanoparticles to preserve their superparamagnetic nature. As a model the histidine-rich protein bovine serum albumin (BSA) was used. The release of the BSA bound to Zn-decorated silica-coated maghemite nanoparticles was analysed using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). We demonstrated that the bonding of the BSA to such modified magnetic nanoparticles is highly reversible and can be controlled by an appropriate change of the external conditions, such as a pH decrease or the presence/supply of other chelating compounds.Entities:
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Year: 2008 PMID: 18400567 DOI: 10.1016/j.jchromb.2008.03.019
Source DB: PubMed Journal: J Chromatogr B Analyt Technol Biomed Life Sci ISSN: 1570-0232 Impact factor: 3.205