RUI: Collaborative Research: Understanding the protein-polysaccharide interactions of natural composite materials in one and two dimensions

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NON-TECHNICAL SUMMARYBiological macromolecules are large molecules which are fundamentally necessary for life such as proteins, carbohydrates, lipids, and nucleic acids. All organisms are composed of a variety of these biomacromolecules, and as such, understanding their molecular interactions is essential for predicting morphology, structure, and function of biomaterials. The study of protein-polysaccharide interactions in biocomposite materials carries implications for fields ranging from medicine to environmental science and materials science. These materials are extremely versatile as shown from a variety of biocomposites used in nature. However, to facilitate deployment of new biocomposite materials in modern technology, the development of new methodologies is required to tune the properties of these materials to suit specific technological demands. The ability to manipulate molecules to form hierarchical structures with precise control, size, spacing, and shape is a central objective of this project in order to enable the rapid fabrication of multi-level structures from single structures. In addition, this project will provide research, training and educational opportunities to high school and undergraduate students for a better understanding of biomaterials science and molecular interactions of biological macromolecules. The proposed research will be seamlessly associated with the needs of the South Jersey undergraduate and K-12 STEM education programs, which will be particularly beneficial for students of engineering, chemistry, physics, biology and computer science backgrounds who are required to undertake research for graduation. Furthermore, this proposal will enable other researchers to use the developed tools and roadmaps for the regeneration of biocomposite materials with critical functionalities and customizable options. TECHNICAL SUMMARYNatural biomacromolecules such as silk and keratin represent structural proteins, while cellulose represents polysaccharides. Understanding their molecular interactions is critical for unleashing a flora of new materials, revolutionizing the way we fabricate multi-structural and multi-functional systems. Knowledge to date is still lacking on how the morphology of various biomacromolecules assemble nor do we understand how their interactions dictate physicochemical properties. Linking morphology modification at the inter- and intra-molecular levels will provide a basic understanding of how the molecular self-assembly progresses and how spatiotemporal morphologies control the structure and physicochemical properties. Achieving this level of understanding and control will be crucial for progress leading to the ability to fabricate robust multi-level structural biocomposites such as 2D films and 1D fibers. It will also help to predict the relationship between protein secondary structures and carbohydrate crystallinity, thus creating potential applications for cellular mechanosensing, cellular regeneration, membrane separation, thermal insulation and energy production. This project hypothesizes that the physicochemical and morphological properties of protein-polysaccharide biocomposites regenerated from ionic liquids are mainly regulated by the formation and dimension of protein secondary structures, glucose-based crystallites, and biomacromolecules backbone-to-backbone chain intercalations. Two main objectives will be pursued to address this hypothesis, including, i) the characterization of protein-polysaccharide materials as a function of molecular structures and processing conditions; ii) understand the relationship between protein secondary structure and cellulose crystallinity in relation to chain intercalation, morphology, and mechanical stability of materials.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.