Design of Silk Biomaterials via Protein Self-Assembly

Natural proteins display critical structural and bioactive properties that have evolved in nature for millions of years. However, depending on the specific protein, there may be useful functions, such as mechanical toughness, while other critical features may be more limiting, such as cell compatibility or a broader range of mechanical properties.<br/>Naturally spun silks supply important fibers for a range of established applications, and in their re-liquified, reconstituted form they also provide increasingly valuable raw materials for the manufacture of a growing range of novel and useful products. Such reconstituted Silk Fibroins (RSF) are now a widespread technology platform. However, they are rather different not only in degree but also in kind to the unprocessed, unspun Native Silk Fibroins (NSF) which are found in the silk gland of the animal prior to spinning. Our research focus on characterization of structural, biophysical and biochemical properties of different types of fiber-forming protein materials including amyloid-based and native silk-based molecular complexes to unveil structure-function relationships, with emphasis on studies related to self-assembled biomaterials. We aim to achieve deep understanding of distinctive properties of fiber-forming protein constructs from atomic to macromolecular levels and molecular pathways from pathological entities to diverse functions to enable expand the concept from soluble proteins to insoluble amyloids, from inhibition to functionalization, and from drugs to new materials.