Large-pore, silica particles with antibody-like, biorecognition sites for efficient protein separation
文献类型:期刊论文
作者 | Zhang, Zulei1,2; Zhang, Xingdi1; Niu, Dechao1; Li, Yongsheng1; Shi, Jianlin1,3 |
刊名 | Journal of Materials Chemistry B
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出版日期 | 2017 |
卷号 | 5期号:22页码:4214-4220 |
ISSN号 | 20507518 |
DOI | 10.1039/c7tb00886d |
英文摘要 | Natural antibodies are used widely for various applications such as in biomedical analysis, protein separation, and targeted-drug delivery, but they suffer from high cost and low stability. In this study, we developed a facile approach for the construction of antibody-like binding sites in a porous silica solid for efficient separation of bovine serum albumin (BSA) based on large-pore silica particles (LPSPs). This was accomplished by grafting two types of organosilane monomers, 3-aminopropyltriethoxylsilane (APTES) and octyltrimethoxysilane (OTMS), to provide hydrogen bonds or hydrophobic interactions with BSA through molecular imprinting technology. The resulting molecularly imprinted, large-pore silica particles (MI-LPSPs) were characterized by scanning electron microscopy (SEM), Fourier transform infrared (FT-IR) spectroscopy, X-ray photoelectron spectroscopy (XPS), thermogravimetric analysis (TG), X-ray diffraction (XRD) and N2sorption analysis. Results showed that the as-synthesized MI-LPSPs exhibited a spherical morphology, favorable stability and large pore structure. The kinetic adsorption experiments showed that the MI-LPSPs could reach equilibrium within one hour and were described well by the pseudo second-order model, indicating that chemical adsorption might be the rate-limiting step. Meanwhile, the MI-LPSPs had a large binding capacity up to 162.82 mg g-1and high selectivity for the recognition of BSA. Moreover, such a high binding capacity and selectivity was retained after six runs, indicating a good stability and reusability of MI-LPSPs. Thus, it is expected that a simple synthetic methodology in the present study provides a promising pathway to prepare novel imprinted materials for efficient purification and separation of target proteins. © 2017 The Royal Society of Chemistry. |
源URL | [http://ir.sic.ac.cn/handle/331005/25555] ![]() |
专题 | 中国科学院上海硅酸盐研究所 |
作者单位 | 1.Lab of Low-Dimensional Materials Chemistry, Key Laboratory for Ultrafine Materials, Ministry of Education, School of Materials Science and Engineering, East China University of Science and Technology, Shanghai; 200237, China; 2.School of Biology and Chemical Engineering, Jiaxing University, Jiaxing; 314001, China; 3.State Key Laboratory of High Performance Ceramics and Superfine Microstructure, Shanghai Institute of Ceramics, Chinese Academy of Sciences, Shanghai; 200050, China |
推荐引用方式 GB/T 7714 | Zhang, Zulei,Zhang, Xingdi,Niu, Dechao,et al. Large-pore, silica particles with antibody-like, biorecognition sites for efficient protein separation[J]. Journal of Materials Chemistry B,2017,5(22):4214-4220. |
APA | Zhang, Zulei,Zhang, Xingdi,Niu, Dechao,Li, Yongsheng,&Shi, Jianlin.(2017).Large-pore, silica particles with antibody-like, biorecognition sites for efficient protein separation.Journal of Materials Chemistry B,5(22),4214-4220. |
MLA | Zhang, Zulei,et al."Large-pore, silica particles with antibody-like, biorecognition sites for efficient protein separation".Journal of Materials Chemistry B 5.22(2017):4214-4220. |
入库方式: OAI收割
来源:上海硅酸盐研究所
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