Prevention of protein adsorption by flexible and rigid chain molecules.

The ability of tethered polymer layers to reduce the non-specific adsorption of proteins is studied using a molecular theory. The protein adsorption isotherms are calculated for flexible and rigid molecules as well as for mixtures. It is found, in agreement with earlier predictions, that flexible polymers are more effective in preventing protein adsorption. The interactions of the polymer with the surface are shown to be very important in determining the ability of the polymer layer to reduce the adsorption of proteins. Further, it is found that one can tune the adsorption of a certain protein conformation by changing the interactions between the surface and the polymer segments or the composition in the case of mixtures. It is found that the optimal layers to obtain large reduction of protein adsorption and availability of functional groups for binding are obtained by using mixtures of flexible and rod-like molecules. The role of the polymer-surface interactions is shown to be different for the kinetic control of protein adsorption as compared to thermodynamic control. The application of the findings as guidelines for the molecular design of biocompatible materials is discussed.