Biofunctional food-derived peptide hydrogels: self-assembly, rheological and bioactive properties, and potential health applications

The intrinsic structures of food proteins and peptides make them relevant in a wide range of applications beyond their basic nutritional roles. For example, peptide self-assembly can be induced by physical or chemical factors, such as pH/temperature induction, chemical crosslinking, and solvent switch methods, to generate supramolecular structures with versatile functionalities. These unique peptides are increasingly explored as novel functional biomaterials for food, biomedical, and pharmaceutical applications. Our studies have combined bioinformatics and peptidomics to discover several self-assembling peptides from plant- and animal-based proteins. Peptide self-assembly was triggered by the solvent-switch or anti-solvent method, and the supramolecular assembly and mechanical properties were characterized using thioflavin T fluorescence, dynamic light scattering, electron microscopy, and rheological analyses. Furthermore, our studies have demonstrated the biological properties and biostability (specifically fibrillar stability) of some of the self-assembled peptides using in-silico, in-vitro and in-vivo models. This presentation also highlights the underlying principles, opportunities, and challenges in the discovery and utilization of bioactive self-assembled food peptides as dual functioning biomaterials for health and biomaterial applications.