Abstract
In this study, bovine serum albumin (BSA) was covalently immobilized onto the surfaces of methyl methacrylate/methyl acrylic acid core–shell latex particles by the carbodiimide method, and the variation of the zeta potential of the BSA–latex complex as a function of the amount of BSA immobilized was measured. The experimental data revealed that the absolute zeta potential of BSA–latex complex exhibited a local minimum at 0.05 mg/m2 of immobilized BSA. A two-layer model for the description of the electrophoretic behavior of the BSA–latex complex is proposed which is capable of explaining the behavior of the variation of the zeta potential as a function of the amount of BSA immobilized.
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