A comparison of the adsorption of three adhesive proteins to biomaterial surfaces.

The adsorption of three cell adhesive proteins with known thrombogenic activity [fibrinogen (FGN), fibronectin (FN), and vitronectin (VN)] was quantified from mono-component protein solutions, from a quaternary-component protein solution, and from plasma and diluted plasma in order to compare their potential for adsorption to polymeric substrates from solutions of varying complexity. The surfaces studied included polyethylene (PE), silicone rubber (SR), Teflon-FEP (FEP), and two polyetherurethanes: one with a poly(tetramethylene oxide) soft segment (PTMO-PU) and one with a poly(ethylene oxide) soft segment (PEO-PU). The adsorption of these proteins from single-component solutions followed the Freundlich isotherm and the adhesive proteins showed similar trends in Freundlich parameters for surfaces of similar surface wettability. Adsorption from a quaternary-component solution composed of physiological molar ratios of the three proteins and human serum albumin (HSA) revealed a significant enrichment of adsorbed vitronectin as determined from ratios of the adsorbed surface fraction of each protein to its respective bulk fraction. The other proteins' adsorption was enriched to a lesser extent in the decreasing order of FGN greater than FN greater than HSA for all surfaces. The relative enrichment of VN from plasma was also high as compared with its bulk concentration, whereas the enrichment of FGN, FN, and HSA was much lower and of approximately the same magnitude. Compared with the three other proteins, VN showed a resistance to displacement from the polymer substrates as either the plasma concentration was increased or the length of contact with plasma and diluted plasma was increased.