The influence of electrostatic forces on protein adsorption.

In this paper we investigate the importance of electrostatic double layer forces on the adsorption of human serum albumin by UV-ozone modified polystyrene. Electrostatic forces were measured between oxidized polystyrene surfaces and gold-coated atomic force microscope (AFM) probes in phosphate buffered saline (PBS) solutions. The variation in surface potential with surface oxygen concentration was measured. The observed force characteristics were found to agree with the theory of electrical double layer interaction under the assumption of constant potential. Chemically patterned polystyrene surfaces with adjacent 5 microm x 5 microm polar and non-polar domains have been studied by AFM before and after human serum albumin adsorption. A topographically flat surface is observed before protein adsorption indicating that the patterning process does not physically modify the surface. Friction force imaging clearly reveals the oxidation pattern with the polar domains being characterised by a higher relative friction compared to the non-polar, untreated domains. Far-field force imaging was performed on the patterned surface using the interleave AFM mode to produce two-dimensional plots of the distribution of electrostatic double-layer forces formed when the patterned polystyrene surfaces is immersed in PBS. Imaging of protein layers adsorbed onto the chemically patterned surfaces indicates that the electrostatic double-layer force was a significant driving force in the interaction of protein with the surface.