Polyphenol-mediated assembly of peptide for engineering functional materials

Abstract

Peptide-based functional materials have garnered significant interests because of their exceptional physicochemical characteristics and diverse functions. In this paper, we have identified four amino acids (arginine, lysine, histidine, and tryptophan) that exhibit high affinity with polyphenols. Then, by adjusting the amount and location of the aforementioned amino acids within peptides, pH of the solution, and the assembly ratio, it is possible to achieve controlled assembly of peptide with polyphenol, 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. Meanwhile, the polyphenol-peptide assemblies can also be finely tuned in terms of their decomposition and protein loading, enabling them to be connected to a variety of bioactivities and stimulus-responsive characteristics. So, the polyphenol-peptide functional materials will be broadly applicable in the future.