Clustering under short-range finite interactions.

In this paper the aggregation of surface modified colloidal particles is presented, paying special attention to the cluster structure and growth. The surface was modified by adsorbing bovine serum albumin (BSA). The interaction potential develops a minimum of restricted depth, weakening the clusters which subsequently restructure and form more compact morphologies. This minimum is responsible for the reversibility of the aggregation processes (this is an important difference between diffusion-limited cluster aggregation and reaction-limited cluster aggregation). The energy minimum is associated with the presence of a steric term in the energy balance, which depends on the size of the adsorbed molecules. BSA molecules with different sizes were employed to test this point. In addition, the short-range interaction seems not to affect significantly the paths of approximating particles, since the aggregation of the clusters at long times is independent of the size of these particles. The long-time kinetics was interpreted in the frame of dynamic scaling concepts. A kinetics model, including surface-surface, protein-surface, and protein-protein aggregation, is used to determine the dominant mechanism controlling the aggregation.