Protein Surface Interactions and Biocompatibility: A Forty Year Perspective

Research in the author’s laboratory on proteins at interfaces over the past four decades, with biocompatibility as the underlying theme, is reviewed. A principal focus in fundamental studies has been the dynamics of adsorbed protein layers in both simple systems and real biofluids. Investigations on protein resistant surfaces based on surface modification with poly(ethylene oxide) and poly(2-methacryloyloxyethyl phosphorylcholine) (polyMPC) have also been a major theme. Most of our work has been done in the context of biomaterials for use in blood contact and the hypothesis that blood compatibility, and biocompatibility in general, depends on control of protein adsorption has guided much of our more recent efforts. Specifically we have hypothesized that surfaces which prevent non-specific protein adsorption and promote specific adsorption of target proteins, should have improved biocompatibility. Blood contacting surfaces that promote fibrinolysis by specific adsorption of plasminogen and tissue plasminogen activator, or that prevent coagulation by adsorption of antithrombin have been investigated on this basis.