Interactionsbetween bovine serum albumin (BSA)/�-lactoglobulin(BLG)/Papain and spherical polyelectrolyte brushes (SPBs) were investigated bya combination of turbidimetric titration, dynamic light scattering (DLS), zetapotential measurement, and small angle x-ray scattering (SAXS) which revealed differentbehaviors, architectures, and phase states of pH dependent protein-SPBinteractions. Binding energetics, affinity, and stoichiometry between BSA/BLG and SPBs weredetermined by isothermal titration calorimetry (ITC). The SPBs consist ofnarrowly distributed polystyrene core particles (ca. 100 nm in diameter) ontowhich linear chains of polyelectrolytes are grafted. The polyelectrolyte shellconsits of either weak anionic poly(acrylic acid) (PAA) or weak cationic poly(2-aminoethylmethacrylate hydrochloride) (PAEMH). For a particular proteins (BSA and BLG), the binding stoichiometry, affinity, architecture, and phase state between proteins and anionic SPBs were significantly different from those for cationic SPBs. Significantly largerbinding affinity and amount were observed for BSA in anionic SPBs versuscationic SPBs, while opposite for BLG, which were explained in terms of thedifferent charge anisotropies of proteins. These findings lay the foundation for SPB applications in the protein purification and selective immobilization of different proteins,enzymes and antibodies. 

Interaction between spherical polyelectrolyte brushes and proteins

247th National Meeting (2014)

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