Understanding the factors regulating biofouling is crucial for the designand implementation of biomaterials. PCBMAbelongs to a family of zwitterionic polymers, where the formation of a stronghydration layer is thought to inhibit protein adsorption. However, amechanistic understanding of how both polymer layer (hydration, charge, etc.)and protein properties (size, charge, 'stiffness', etc.) affectsprotein-surface interactions is largely ill-defined. In this study, weare presenting a comprehensive thermodynamic profile for the adsorption ofHuman Serum Albumin (HSA) and a-lactalbumin onto PCBMA-NPs with chains varyingin end-group chemistry (phosphonate and TEMPO) and spacer-group length in thezwitterion. In general, preliminary results indicate that protein adsorption ontoPCBMA-NPs is entropically-driven; with electrostatic forces playing the mainrole in a-lactalbumin adsorption and hydrophobic interactions being importantin HSA adsorption. Furthermore, calorimetric studies suggest that maintainingwater molecules within the polymer-protein interface may largely inhibitprotein adsorption.

Protein adsorption onto poly-carboxybetaine
methacrylamide (PCBMA)-grafted Si nanoparticles (NPs): A thermodynamic investigation

243rd National Meeting (2012)

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Protein adsorption onto poly-carboxybetaine methacrylamide (PCBMA)-grafted Si nanoparticles (NPs): A thermodynamic investigation