文献类型：期刊文献

英文题名：Binding between Proteins and Cationic Spherical Polyelectrolyte Brushes: Effect of pH, Ionic Strength, and Stoichiometry

作者：Wang, Siyi[1];Chen, Kaimin[1,2];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

年份：2013

卷号：14

期号：3

起止页码：818

外文期刊名：BIOMACROMOLECULES

收录：;EI(收录号：20131216128186);WOS:【SCI-EXPANDED(收录号:WOS:000316044700027)】；

基金：We gratefully acknowledge the National Natural Science Foundation of China (No. 51273063), the Fundamental Research Funds for the Central Universities, the higher school specialized research fund for the doctoral program (20110074110003), and the China Postdoctoral Science Foundation (2012M511088) for support to this work.

语种：英文

外文关键词：Dynamic light scattering - Ionic strength - Polyelectrolytes - Antibodies - Body fluids - Stoichiometry - Enzyme immobilization

摘要：Cationic spherical polyelectrolyte brushes (SPBs) were synthesized by photoemulsion polymerization, consisting of a polystyrene core with a diameter around 80 nm and a poly(2-aminoethylmethacrylate hydrochloride) (PAEMH) shell with a thickness from 10 to 50 nm densely grafted on the core surface. The binding of various proteins onto SPBs was observed by turbidimetric titration, dynamic light scattering (DLS), zeta potential, and isothermal titration calorimetry (ITC). The binding, aggregation, and releasing of proteins by SPB can be tuned by modulating pH. The pH regions of binding for bovine serum albumin (BSA), beta-lactoglobulin (BLG), and papain onto SPBs are markedly different and tunable by ionic strength and stoichiometry between protein and SPB. Binding energetics, affinity, and amount of various proteins onto cationic SPBs were determined by ITC. These findings lay the foundation for SPB applications in the protein purification and selective immobilization of different proteins, enzymes, and antibodies