Hydrophilic poly(ethylene glycol) (PEG)- and zwitterionic poly(sulfobetaine methacrylate) (pSBMA)-based materials have been widely used in drug-delivery systems due to their super-lowfouling capacity. However, molecular interactions between proteins and these two polymers remain elusive, although both polymers can achieve similar antifouling performance. Here, we develop systematic ways to examine and compare the conformational changes and surface binding of different proteins (BSA and Lysozyme) upon interacting with PEG and pSBMA materials using multiple spectroscopic techniques including NMR, AFM, SPR, and ATR-FTIR. It was observed that polymer-induced conformational change of proteins affects the activity and binding of adsorbed proteins. Additionally, we also investigate the effects of polymer molecular weights and polymer concentrations on protein-polymer interactions. This work provides new insights into the fundamental understanding of protein-polymer interactionsunderlying protein catalysis, protein engineering and design, and protein drugs.

Comparative study of protein adsorption, conformation, and binding at PEG and PolySBMA interfaces

245th National Meeting (2013)

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