In situ studies on protein adsorption onto a poly(2-methoxyethylacrylate) surface by a quartz crystal microbalance

We have reported that poly(2-methoxyethylacrylate) (PMEA) showed excellent blood compatibility though it had a simple chemical structure, and have bee n making efforts to clarify the reason for the blood compatibility. It is w ell-known that the adsorption behavior of the protein affects the compatibi lity. Therefore, the adsorption behaviors of bovine serum albumin (BSA) and human fibrinogen onto the surfaces of PMEA, poly(2-hydroxyethyl methacryla te) (PHEMA) and polypropylene (PP) were investigated by using a quartz crys tal microbalance (QCM), where PHEMA and PP were selected as the representat ives of hydrophilic and hydrophobic polymers, respectively. Both proteins w ere observed to adsorb onto all the polymer surfaces according to Langmuir' s adsorption isotherm. The maximum adsorption amounts and the apparent asso ciation constants of the proteins for PMEA obtained from the isotherm were lower than those for PHEMA and PP. These results suggest that the interacti on between PMEA and the proteins is weaker than the interaction with PP and PHEMA. (C) 2001 Elsevier Science B.V. All rights reserved.