A Comprehensive Review of Self-Assembled Food Protein-Derived Multicomponent Peptides: From Forming Mechanism and Structural Diversity to Applications

Abstract

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.

Peptide Supramolecular Self-Assembly: Regulatory Mechanism, Functional Properties, and Its Application in Foods

“…Food-derived natural peptides with abundant bioactivities have been widely studied in the field of food. , Recently, researchers have found that food-derived natural peptides with remarkable structural and functional characteristics could self-assemble into multidimensional structures to thereby produce specific health benefits . Marques et al showed that cowpea peptides could self-assemble into micelle structures with impressive antioxidant activity through measurements of oxygen radical absorption capacity.…”

“…In recent years, researchers have reviewed the synergies of various noncovalent interactions involved in the self-assembly process, , which are necessary to determine thermodynamically stable structures. In fact, individual amino acids such as Phe or Ser can form oligomers, clusters, or even toxic fiber aggregates in solution with various noncovalent interactions, which hints at the mechanism of peptide assembly and growth trends .…”

Self-Assembly of Metabolite Nanostructures toward Functional Biomaterials

“…The self-assembly of metabolites results in the spontaneous formation of an ordered nanostructure guided by thermodynamics and dynamics. 48 In the self-assembly process, noncovalent interactions, including hydrophobic interactions, hydrogen bonding, π−π stacking, and electrostatic interactions, cause the monomers to spontaneously assemble into a stable structure with a specific regular geometric appearance (Figure 2). 49 These noncovalent interactions can affect the structures and functions of the assemblies, even though they are weak.…”

“…Electrostatic interactions refer to the force generated by the interaction of electric charges, including electrostatic attraction and repulsion, which are nondirectional and have a low binding energy. 48 These interactions are essential for maintaining the structural stability of biomolecules and realizing biological functions. Because of the weak acid and base properties of the COOH and NH 2 , the pH of the solution can be adjusted to affect the electrostatic interactions.…”

“…Noncovalent interactions are prevalent both between and within molecules and play a vital role in life activities and molecular self-assembly. The self-assembly of metabolites results in the spontaneous formation of an ordered nanostructure guided by thermodynamics and dynamics . In the self-assembly process, noncovalent interactions, including hydrophobic interactions, hydrogen bonding, π–π stacking, and electrostatic interactions, cause the monomers to spontaneously assemble into a stable structure with a specific regular geometric appearance (Figure ).…”