Protein adsorption to polymer particles: role of surface properties.

Adsorption isotherms of four plasma proteins (fibrinogen, IgG, human serum albumin, and bovine serum albumin) using four different types of small particles as substrates (siliconized glass, Teflon, polyvinylchloride, and Nylon-6,6) are reported. The suspending liquid medium was phosphate-buffered saline, with a surface tension higher than that of any of the proteins. In keeping with the thermodynamic expectations for these systems, protein adsorption decreases for all solids in sequence from fibrinogen (the most hydrophobic) to IgG, human serum albumin, and bovine serum albumin (the most hydrophilic). Furthermore, the extent of protein adsorption also decreases from the low surface tension (hydrophobic) to the higher surface tension solids, again as expected on thermodynamic grounds. There is one minor yet interesting exception to the thermodynamic pattern: In spite of the slightly lower surface tension of siliconized glass, the extent of protein adsorption is slightly higher to Teflon than to siliconized glass. This result is attributed to the theoretically well known phenomenon of "screening."