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

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. Th...

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Bibliographic Details
Published in:Biomacromolecules 2013-03, Vol.14 (3), p.818-827
Main Authors: Wang, Siyi, Chen, Kaimin, Li, Li, Guo, Xuhong
Format: Article
Language:English
Subjects:
Adsorption
Animals
Applied sciences
Biological and medical sciences
Calorimetry
Cattle
Exact sciences and technology
Fundamental and applied biological sciences. Psychology
Hydrogen-Ion Concentration
Lactoglobulins - chemistry
Methacrylates - chemistry
Molecular biophysics
Osmolar Concentration
Physicochemistry of polymers
Polyamines - chemical synthesis
Polyamines - pharmacokinetics
Polymerization
Polymers and radiations
Polystyrenes - chemistry
Proteins - chemistry
Serum Albumin, Bovine - chemistry
Surface properties. Adsorption
Thermodynamics
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Summary: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.
ISSN:1525-7797
1526-4602
DOI:10.1021/bm301865g