Physico-chemical characterization of bovine serum albumin in solution and as deposited on surfaces.

The interactions between proteins and solid surfaces are important for the formation of biocompatible materials. In this study, the physicochemical properties of Bovin serum albumin (BSA) in solution and on a solid surface were studied. The zeta potential and number of uncompensated charges on BSA surfaces were determined from electrophoretic mobility measurements. The dynamic viscosity was also measured to determine BSA conformations in solution, and the data were converted to the effective length L(ef) of the BSA molecule. The length of a BSA molecule was measured to be 8.3 nm in the compact state (N form at pH 4-9) and 26.7 nm in the extended state (F-form). This study demonstrates that the relationship between the hydrodynamic radius, dynamic viscosity and electrophoretic mobility can provide information about the shape and conformation of biopolymer in solution. The contact angle measurements and deposition of fluorescent latex particles were used to characterise BSA monolayers on a mica surface, which were produced by controlled adsorption under diffusion transport. The results suggest that the distribution of charge across a BSA molecule is heterogeneous as evidenced by the presence of positive and negative patches. The maximum contact angle was observed under conditions in which both BSA and mica were oppositely charged. A higher positive zeta potential of BSA was observed to correlate with a higher contact angle. However, at a higher negative zeta potential, BSA exhibited a lower binding affinity. The charge distribution across BSA monolayers was also studied via the colloidal deposition method using negatively charged fluorescent latex particles. Unexpectedly, the fluorescent latex particles adsorbed onto BSA monolayers, even when the effective zeta potential of BSA was negative. This phenomenon may originate from the heterogeneous charge distribution across BSA molecules.