Protein self-assembly on surfaces, interfaces and nanoparticles

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Surfaces such as those presented by an air-liquid interface or air-borne nanoparticles exert significant effects on protein aggregation in biological environments. We will develop a comprehensive theoretical and experimental approach to study the effects of such surfaces on the self assembly of proteins leading to disease causing amyloid fibrils. This will provide a molecular level understanding of protein self-association and a rational basis for the design of inhibitors to stop protein aggregation. The work will also establish design principles for new nanomaterials via the controlled self assembly of proteins on surfaces.