文献类型：期刊文献

英文题名：Protein immobilization and separation using anionic/cationic spherical polyelectrolyte brushes based on charge anisotropy

作者：Wang, Siyi[1];Chen, Kaimin[1,2];Xu, Yisheng[1,3];Yu, Xuanji[1];Wang, Weihua[1];Li, Li[1];Guo, Xuhong[1]

机构：[1]E China Univ Sci & Technol, State Key Lab Chem Engn, Shanghai 200237, Peoples R China;[2]Shanghai Jiao Tong Univ, Med X Res Inst, Shanghai 200030, Peoples R China;[3]Cornell Univ, Ithaca, NY 14853 USA

年份：2013

卷号：9

期号：47

起止页码：11276

外文期刊名：SOFT MATTER

收录：;EI(收录号：20134917042615);WOS:【SCI-EXPANDED(收录号:WOS:000327499900017)】；

基金：We gratefully acknowledge the National Natural Science Foundation of China (no. 51273063 and 11076002/A06), the Fundamental Research Funds for the Central Universities, the higher school specialized research fund for the doctoral program (20110074110003), the China Postdoctoral Science Foundation (12Z102060005), and Shanghai Synchrotron Radiation Facility for support to this work.

语种：英文

外文关键词：Anisotropy - Body fluids - Dynamic light scattering - Titration - Phospholipids - Binding energy - Stoichiometry - X ray scattering

摘要：Interactions between bovine serum albumin (BSA)/b-lactoglobulin (BLG) and spherical polyelectrolyte brushes (SPBs) were investigated by a combination of turbidimetric titration, dynamic light scattering (DLS), zeta potential measurement, and small angle X-ray scattering (SAXS) which revealed different behaviors, architectures, and phase states of pH dependent protein-SPB interactions. Binding energetics, affinity, and stoichiometry between BSA-BLG and SPBs were determined by isothermal titration calorimetry (ITC) to get further information concerning the interaction difference. The SPBs consist of narrowly distributed polystyrene core particles (ca. 80 nm in diameter) onto which linear chains of polyelectrolytes, either weak anionic poly(acrylic acid) (PAA) or weak cationic poly(2-aminoethyl methacrylate hydrochloride) (PAEMH), are grafted. For a particular protein (BSA or BLG), the binding stoichiometry, affinity, architecture, and phase state between proteins and anionic SPBs were significantly different from those for cationic SPBs. Significantly larger binding affinity and adsorbed amount were observed for BSA in anionic SPBs versus cationic SPBs, while opposite for BLG, which were explained in terms of different charge anisotropy of proteins. These findings lay the foundation for SPB applications in the separation and immobilization of different proteins.