The self-assembly of globular protein-polymer diblock copolymers into nanostructured phases provides a route for the construction of biofunctional materials with a high density of active protein domains. The thermodynamics of self-assembly in aqueous environments and in solid-state materials shows significant complexity due to the complex shapes and interactions present in folded protein blocks. Herein, we isolate the effect of protein surface interactions on the self-assembly process through comparisons of self-assembly in structurally homologous proteins with significantly different surface potentials. It is demonstrated that under neutral solvent conditions coarse-grained effects dominate the self-assembly process; however, the details of the protein interaction have a larger effect under conditions where the buffer is selective for the protein block. Experiments with varying ionic strength suggest that ionic interactions promote phase separation in the systems studied. Changes in polymer chemistry are also explored as a method to alter protein-polymer interactions, demonstrating a very large impact on self-assembly in concentrated solution, including the observation of new cubic nanodomain structures. Finally, coating materials into thin films enables is shown as a way to produce biocatalytically active materials and coatings. 

Effect of protein interactions on the self-assembly of globular protein-polymer diblock copolymers

247th National Meeting (2014)

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