A major challenge in biotechnology is the identification of material properties that enhance or shut down protein functions in hybrid bio-materials. This talk describes a new approach, Fast Relaxation Imaging (FReI) that enables the direct imaging of protein folding stability in situ in biomaterials at diffraction-limited spatial resolution. This approach combines fluorescence resonance energy transfer (FRET) to visualize protein conformations in situ with localized temperature jumps to assess the impact of material microenvironments on protein folding stability. Initial results described in this talk investigated the interplay between crowding and cross-linking density on the folding stability of a model protein phosphoglycerate kinase and a crowding sensor within polyacrylamide hydrogels. These results demonstrated how the interplay between protein crowding and polymer interactions affects protein stability at different polyacrylamide cross-linking densities. The FReI measurements open up new opportunities to investigate protein/material interactions that will identify new design rules for protein-compatible materials at an unprecedented level of detail.

Direct measurements of protein folding stability in biomaterials

255th National Meeting (2018)

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