Food protein-derived multicomponent peptides (FPDMPs) are a natural blend of numerous peptides with various bioactivities and multiple active sites that can assume several energetically favorable conformations in solutions. The remarkable structural characteristics and functional attributes of FPDMPs make them promising codelivery carriers that can coassemble with different bioactive ingredients to induce multidimensional structures, such as fibrils, nanotubes, and nanospheres, thereby producing specific health benefits. This review offers a prospective analysis of FPDMPs-based self-assembly nanostructures, focusing on the mechanism of formation of self-assembled FPDMPs, the internal and external stimuli affecting peptide self-assembly, and their potential applications. In particular, we introduce the exciting prospect of constructing functional materials through precursor template-induced self-assembly of FPDMPs, which combine the bioactivity and self-assembly capacity of peptides and could dramatically broaden the functional utility of peptide-based materials.
Keywords: Enzymatic hydrolysis; Multicomponent peptides; Noncovalent interactions; Nutraceuticals delivery; Self-assembly.