THE ADSORPTION AND ELUTABILITY OF ALBUMIN, IGG, AND FIBRONECTIN ON RADIOFREQUENCY PLASMA DEPOSITED POLYSTYRENE

Because protein adsorption is extremely rapid, cells seeded on a substrate in culture medium containing serum are more likely to interact with an adsorbed protein layer than to make direct contact with the surface. Therefore, the composition of the protein layer adsorbed from serum and the conformation of the protein molecules are probably important factors for later cellular events. We measured albumin and IgG adsorption from 10% serum onto polystyrene substrates that had been modified by radiofrequency plasma deposition from mixtures of oxygen and acetone vapor. Despite different surface chemistries, all treated substrates adsorb similar amounts of albumin and IgG from serum. However, the resistance of both adsorbed proteins to elution by sodium dodecyl sulfate was found to increase with the oxygen content of the substrates. In addition, when the treated surfaces are precoated with pure solutions of albumin or IgG, the subsequent binding of fibronectin increases with surface oxygen. © 1991.