I will present new research that addresses the major challenge of identifying material properties that alter bio-macromolecule folding stability abiotic environments. How proteins interact with materials impacts a wide range of applications, from drug delivery to ship paints. A major goal of our work is to identify the molecular scale properties of materials that alter protein stability and function.
Recent studies of protein interactions with zwitterionic polymers and with temperature responsive poly(N-isopropyl acrylamide) (pNIPAM) challenge widespread views of polymers long thought to be protein compatible and non fouling (protein resistant). Fluorescence measurements of polymer/protein interactions produced surprising results. Despite a common view that poly zwitterions such as poly(sulfobetaine) (pSB) are ‘super low fouling’, soluble pSB binds and destabilizes proteins in solution. Proteins also adsorb on pSB thin films, and the non monotonic dependence on polymer coverage hints at the underlying adsorption mechanism.
Proteins similarly adsorb on pNIPAM, above the lower critical solution temperature where the chains are ‘sticky’ to proteins. Recent work with Martin Gruebele (Chemistry, U of Illinois) extended a fluorescence based approach, to quantify the impact of the polymer micro environments on protein stability, at submicron spatial resolution and millisecond time resolution. Surprising findings reveal that pNIPAM stabilizes adsorbed protein above the LCST. These results reveal unexpected ways that polymers perturb proteins and open up new avenues for identifying material properties that preserve or shut down protein function.
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