Chemical Physics Seminar: Protein self-assembly and its association with material properties
Dr. Ulyana Shimanovich, Weizmann Institute of Science
Molecular self-assembly in proteins is the basis of phenomena ranging from the construction of materials for nanotechnology to the formation of molecular machinery within living cells. An important class of molecular structures that emerges from the self-assembly of simpler components is that of filamentous assemblies of biological macromolecules. 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.
Naturally spun silks supply important fibers for a range of established applications, and in their re-liquified, the 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 focuses on the 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 a 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.