In this work, the aggregation behaviour of surface-modified colloidal particles was studied. In view of this, a method was developed which allows the dynamic scaling functions s(t) and Phi(x) to be calculated from single-cluster light scattering data. The method was employed to investigate the aggregation of colloidal particles covered with different amounts of bovine serum albumin (BSA). It was found that BSA molecules do not alter the aggregation regime when the samples aggregate at the protein's isoelectric point. Far from this condition, however, the adsorbed protein molecules increase the residual electrostatic interaction and the aggregation regime changes from diffusion- to reaction-controlled aggregation. [References: 9]
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