Large-pore, silica particles with antibody-like, biorecognition sites for efficient protein separation
Zhang, Zulei1,2; Zhang, Xingdi1; Niu, Dechao1; Li, Yongsheng1; Shi, Jianlin1,3
Source PublicationJournal of Materials Chemistry B
AbstractNatural 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.
EI Accession Number20172803923167
EI KeywordsX ray photoelectron spectroscopy
EI Classification Number461.2 Biological Materials and Tissue Engineering - 461.9.1 Immunology - 801 Chemistry - 802.3 Chemical Operations - 931.2 Physical Properties of Gases, Liquids and Solids
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Cited Times:9[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Affiliation1.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
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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.
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