A General and Convenient Peptide Self-Assembling Mechanism for Developing Supramolecular Versatile Nanomaterials Based on The Biosynthetic Hybrid Amyloid-Resilin Protein

Self-assembling peptides are valuable building blocks to fabricate supramolecular biomaterials, which have attracted great attention due to their broad applications ranging from biomedicine to biotechnology. However, the limited choice of an analogous method to induce a desired set of globular proteins into peptide hydrogels hinders these designs. In addition, it is vital to impart numerous macroscopic material properties in one material, which are essential for successful tissue engineering or biomedical applications. Here, an easy-to-implement and tunable self-assembling strategy, which employs Ure2 amyloidogenic peptide, was described to induce any target proteins of choice to assemble into supramolecular hydrogels alone or in combination with notable compositional control. Furthermore, through fusing the amyloidogenic peptide with different kinds of resilin-like polypeptides, the collective effect of nanoscale interactions among amyloid nanofibrils and partially disordered elastomeric polypeptides, which consisted of folded globular GB1 domain and a consensus repeat from the unstructured resilin, was investigated. This led to many useful macroscopic material properties simultaneously emerging from one pure protein material, i.e., strong adhesion to any substrates under wet conditions, rapidly self-assembling into robust and porous hydrogels, adaptation to remodeling processes, strongly promoting cell adhesion, proliferation and differentiation. Moreover, we demonstrated this supramolecular material's robust performance in vitro and vivo for tissue engineering, cosmetic and hemostasis applications and exhibited superior performance compared to corresponding commercial counterparts. To the best of our knowledge, few pure protein-based materials could meet such seemingly mutually exclusive properties simultaneously. Such versatility renders this novel supramolecular nanomaterial as next-generation functional protein-based materials, and we demonstrated the sequence level modulation of structural order and disorder as an untapped principle for the design of new proteins.