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ABSTRACT: By combining turbidimetric titration, dynamic light scattering (DLS), and zeta potential methods, we demonstrated that the adsorption of bovine serum albumin (BSA) in annealed cationic spherical polyelectrolyte brushes (SPB) can be controlled by modulating the pH, ionic strength, BSA concentration of the mixed solution, and SPB thickness. The SPB consist of a polystyrene core with a diameter around 80nm and a dense shell of poly (2-aminoethylmethacrylate hydrochloride) (PAEMH) with a thickness from 10 to 60nm covalently attached on the core surface. Results revealed the existence of three pH regions, corresponding to (1) adsorption of BSA in SPB, (2) aggregation of SPB induced by BSA adsorption, and (3) desorption of BSA from SPB. The extent of the pH regions can be modulated by ionic strength, BSA concentration, or SPB thickness. Adsorption measurements demonstrated that the adsorbed amount of BSA in SPB was affected by pH, ionic strength, and SPB thickness. These findings lay the foundation for protein separation by SPB.
Colloids and surfaces. B, Biointerfaces 02/2013; · 2.60 Impact Factor
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ABSTRACT: 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), β-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.
Biomacromolecules 02/2013; · 5.48 Impact Factor
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[show abstract]
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ABSTRACT: By combining turbidimetric titration, dynamic light scattering (DLS), and zeta potential methods, we demonstrated that the adsorption of bovine serum albumin (BSA) in annealed cationic spherical polyelectrolyte brushes (SPB) can be controlled by modulating the pH, ionic strength, BSA concentration of the mixed solution, and SPB thickness. The SPB consist of a polystyrene core with a diameter around 80 nm and a dense shell of poly (2-aminoethylmethacrylate hydrochloride) (PAEMH) with a thickness from 10 to 60 nm covalently attached on the core surface. Results revealed the existence of three pH regions, corresponding to (1) adsorption of BSA in SPB, (2) aggregation of SPB induced by BSA adsorption, and (3) desorption of BSA from SPB. The extent of the pH regions can be modulated by ionic strength, BSA concentration, or SPB thickness. Adsorption measurements demonstrated that the adsorbed amount of BSA in SPB was affected by pH, ionic strength, and SPB thickness. These findings lay the foundation for protein separation by SPB.
Colloids and Surfaces B Biointerfaces 02/2013; · 3.46 Impact Factor
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4th International Conference on Biomedical Engineering and Informatics, BMEI 2011, Shanghai, China, October 15-17, 2011; 01/2011
