文献类型：期刊文献

英文题名：Large-pore, silica particles with antibody-like, biorecognition sites for efficient protein separation

作者：Zhang, Zulei[1,2];Zhang, Xingdi[1];Niu, Dechao[1];Li, Yongsheng[1];Shi, Jianlin[1,3]

机构：[1]East China Univ Sci & Technol, Sch Mat Sci & Engn, Lab Low Dimens Mat Chem, Key Lab Ultrafine Mat,Minist Educ, Shanghai 200237, Peoples R China;[2]Jiaxing Univ, Sch Biol & Chem Engn, Jiaxing 314001, Peoples R China;[3]Chinese Acad Sci, Shanghai Inst Ceram, State Key Lab High Performance Ceram & Superfine, Shanghai 200050, Peoples R China

年份：2017

卷号：5

期号：22

起止页码：4214

外文期刊名：JOURNAL OF MATERIALS CHEMISTRY B

收录：;EI(收录号：20172803923167);WOS:【SCI-EXPANDED(收录号:WOS:000403026400022)】；

基金：This study was financially supported by the National Key Research and Development Program of China (Grant No. 2016YFA0203700), National Natural Science Foundation of China (501100001809) (Grant No. 51572083, 5141101086, 51472085), Shanghai Rising-Star Program (16QA1401300), Shanghai Chenguang project (13CG25), 111 project (B14018), and The Fundamental Research Funds for the Central Universities.

语种：英文

外文关键词：Binding sites - Thermogravimetric analysis - X ray diffraction - Body fluids - Silica - Fourier transform infrared spectroscopy - Scanning electron microscopy - Separation - Targeted drug delivery - X ray photoelectron spectroscopy - Hydrogen bonds - Reusability - Controlled drug delivery - Hydrophobicity

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 N-2 sorption 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(-1) and 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.