This project investigated how protein-based materials assemble across multiple length scales, focusing on how early structural organization influences the formation of fibers and gels. Protein assembly is central to both biological and industrial materials, from silk fibers to plant-based food systems, yet the pathways linking molecular structure to macroscopic properties remain poorly understood. By studying both silk proteins and yellow pea protein systems, this work addressed how processing conditions, solvent environments, and component interactions govern assembly pathways and final material properties.
Neutron scattering techniques played a central role in resolving structural evolution across length scales within the same sample. Time-resolved small-angle neutron scattering, combined with complementary spectroscopic methods, enabled the identification of intermediate structures in silk fibroin prior to β-sheet formation, demonstrating that assembly pathways are selected by environmental conditions rather than being fixed. Contrast-variation neutron scattering further allowed selective observation of different components in complex pea protein–starch mixtures, revealing how thermal processing drives co-assembly depending on prior history. These neutron-based approaches were complemented by small-angle X-ray scattering and modelling to link solution-state organization to protein architecture.
Overall, the findings demonstrate that the properties of protein-based materials are largely determined at early, pre-gelation stages through pathway-dependent intermediates and solvent-mediated interactions. By establishing multimodal neutron and X-ray scattering as powerful tools for tracking hierarchical assembly, this work provides a framework for designing protein-based materials with tailored properties. The insights are directly relevant for developing sustainable biomaterials, improving plant-based food textures, and advancing bioinspired fiber technologies, where precise control over structure formation is critical for performance and functionality.