Zinc-decorated silica-coated magnetic nanoparticles for protein binding and controlled release

被引:29
作者
Bele, Marjan [1 ]
Hribar, Gorazd [1 ]
Campelj, Stanislav [2 ]
Makovec, Darko [2 ]
Gaberc-Porekar, Vladka [1 ]
Zorko, Milena [1 ]
Gaberscek, Miran [1 ]
Jamnik, Janko [1 ]
Venturini, Peter [1 ]
机构
[1] Natl Inst Chem Slovenia, Ljubljana 1000, Slovenia
[2] Jozef Stefan Inst, Ljubljana 1000, Slovenia
来源
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES | 2008年 / 867卷 / 01期
关键词
magnetic nanoparticles; silica coating; zinc adsorption; histidine affinity binding; protein binding; protein nanoparticles; coordinative binding;
D O I
10.1016/j.jchromb.2008.03.019
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 histicline-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. (C) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码:160 / 164
页数:5
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