Uncovering scaling laws for force labile proteins to enable the design of smart biomaterials

Protein hydrogels are a relatively new type of biomaterial known for providing interesting viscoelastic properties, including mimicking mechanical properties of human cartilage and built-in biological functionality. In this new study we focus on determining if colloidal or polymeric scaling laws can be used to describe a protein gel network which is built from a force labile, mechanically compliant protein building block. It has been hypothesized that the coil-like unfolded proteins occupy the intercluster region thereby contributing positively to the mechanics of the gels. We propose to use SANS to investigate the network structure of photochemically crosslinked force labile Bovine Serum Albumin (BSA) hydrogels at varying protein volume fraction (ϕ). We will interrogate the data utilising our previously described fractal structure model to extract key structural parameters such as correlation lengths and fractal dimensions of fractal protein clusters, to examine how these clusters vary in size, shape, and density as a function of ϕ crucial to determine the scaling laws (useful for gel design) and mesh size (useful for drug delivery).