Polyphenol-mediated assembly of peptides for engineering functional materials

Peptide-based functional materials have garnered significant interest because of their exceptional physicochemical characteristics and diverse functions. In this study, we identified four amino acids (arginine, lysine, histidine, and tryptophan) that exhibit high affinity with polyphenols. By adjusting the amount and location of these amino acids within peptides, the pH of the solution, and the assembly ratio, it is possible to achieve controlled assembly of peptides with polyphenols, including whether or not it can be assembled as well as the size and morphology of the assemblies. This approach also allows us to manipulate both the formation of assemblies and their size and morphology. The polyphenol-peptide assemblies can be finely tuned in terms of their decomposition and protein loading, enabling their connection to a variety of bioactivities and stimulus-responsive characteristics. The results indicate that the polyphenol-peptide functional materials will be broadly applicable in the future.