Preparation of Fe3O4@SiO2@Layered Double Hydroxide Core-Shell Microspheres for Magnetic Separation of Proteins

被引:758
作者
Shao, Mingfei [1 ]
Ning, Fanyu [1 ]
Zhao, Jingwen [1 ]
Wei, Min [1 ]
Evans, David G. [1 ]
Duan, Xue [1 ]
机构
[1] Beijing Univ Chem Technol, State Key Lab Chem Resource Engn, Beijing 100029, Peoples R China
基金
中国国家自然科学基金;
关键词
LAYERED DOUBLE HYDROXIDES; PURIFICATION; HISTIDINE; NANOPARTICLES; BINDING; CHROMATOGRAPHY; HYDROTALCITE; STABILITY; EXCHANGE; REMOVAL;
D O I
10.1021/ja2086323
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Three-component microspheres containing an SiO2-coated Fe3O4 magnetite core and a layered double hydroxide (LDH) nanoplatelet shell have been synthesized via an in situ growth method. The resulting Fe3O4@SiO2@NiAl-LDH microspheres display three-dimensional core-shell architecture with flowerlike morphology, large surface area (83 m(2)/g), and uniform mesochannels (4.3 nm). The Ni2+ cations in the NiAl-LDH shell provide docking sites for histidine and the materials exhibit excellent performance in the separation of a histidine (His)-tagged green fluorescent protein, with a binding capacity as high as 239 mu g/mg. The microspheres show highly selective adsorption of the His-tagged protein from Escherichia coli lysate, demonstrating their practical applicability. Moreover, the microspheres possess superparamagnetism and high saturation magnetization (36.8 emu/g), which allows them to be easily separated from solution by means of an external magnetic field and subsequently reused. The high stability and selectivity of the Fe3O4@SiO2@NiAl-LDH microspheres for the His-tagged protein were retained over several separation cycles. Therefore, this work provides a promising approach for the design and synthesis of multifunctional LDH microspheres, which can be used for the practical purification of recombinant proteins, as well as having other potential applications in a variety of biomedical fields including drug delivery and biosensors.
引用
收藏
页码:1071 / 1077
页数:7
相关论文
共 37 条
[1]   Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins [J].
Arnau, Jos ;
Lauritzen, Conni ;
Petersen, Gitte E. ;
Pedersen, John .
PROTEIN EXPRESSION AND PURIFICATION, 2006, 48 (01) :1-13
[2]  
Choudary BM, 2001, ANGEW CHEM INT EDIT, V40, P763, DOI 10.1002/1521-3773(20010216)40:4<763::AID-ANIE7630>3.0.CO
[3]  
2-T
[4]   Intercalative nanohybrids of nucleoside monophosphates and DNA in layered metal hydroxide [J].
Choy, JH ;
Kwak, SY ;
Park, JS ;
Jeong, YJ ;
Portier, J .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1999, 121 (06) :1399-1400
[5]   High-performance affinity chromatography for the purification of heparin-binding proteins from detergent-solubilized smooth muscle cell membranes [J].
Clairbois, AS ;
Letourneur, D ;
Muller, D ;
Jozefonvicz, J .
JOURNAL OF CHROMATOGRAPHY B, 1998, 706 (01) :55-62
[6]   Superparamagnetic high-magnetization microspheres with an Fe3O4@SiO2 core and perpendicularly aligned mesoporous SiO2 shell for removal of microcystins [J].
Deng, Yonghui ;
Qi, Dawei ;
Deng, Chunhui ;
Zhang, Xiangmin ;
Zhao, Dongyuan .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2008, 130 (01) :28-+
[7]   Separation used for purification of recombinant proteins [J].
Dyr, JE ;
Suttnar, J .
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES, 1997, 699 (1-2) :383-401
[8]  
Fogg AM, 1999, ADV MATER, V11, P1466, DOI 10.1002/(SICI)1521-4095(199912)11:17<1466::AID-ADMA1466>3.0.CO
[9]  
2-1
[10]   Macroscopically ordered hydrotalcite-type materials using self-assembled colloidal crystal template [J].
Géraud, E ;
Prévot, V ;
Ghanbaja, J ;
Leroux, F .
CHEMISTRY OF MATERIALS, 2006, 18 (02) :238-240