Induction of multicomponent peptide assembly via solvent exchange strategy for enhanced structure and bioactivities

Multicomponent peptides, composed of numerous peptides with various binding sites and functionalities, are increasingly exploited in nanotechnology, biomedicine and functional food applications. This article reported that nucleation and growth of Zein (Z) during solvent exchange could form a confined space to drive spontaneous self-assembly of multicomponent peptides. The self-assembly process began with a concentration gradient generated by the exchange of water and ethanol driving the nucleation of Z to form small aggregates, while multicomponent peptides selectively or anisotropically adsorbed on the Z surface via electrostatic interactions and hydrophobic interactions, participating in and controlling the assembly kinetics, ultimately leading to the formation of well-defined nanoparticles (NPs). The multicomponent peptides-based assemblies could effectively encapsulate the hydrophobic functional agent quercetin (Que), presenting good biocompatibility, antioxidant activity, and preventing DSS-induced colitis. This study elucidated the self-assembly mechanism of multicomponent peptides and demonstrated their synergistic effects with hydrophobic compounds for disease prevention, offering valuable insights into the development of novel functional materials to regulate human health.