Precursor template-induced egg white-derived peptides self-assembly for the enhancement of curcumin: Structure, environmental stability, and bioavailability

[Display omitted] •Precursor template Z-HA NPs induced EWDP self-assembly into well-defined structures.•Bioactivity and self-assembly properties of EWDP was simultaneously leverage.•The self-assembled EWDP reinforced the Cur' physio-chemical stability.•The self-assembled EWDP exert synergistic antioxidant activity with Cur.•The self-assembled EWDP enhance the bioaccessibility of Cur by boosting solubility. Natural multicomponent peptides with abundant bioactivity, varied sizes, and tunable interaction potential are available for rational designing novel self-assembled delivery carriers. Herein, we exploited zein-hyaluronic acid nanoparticles (Z-HA NPs) with a predetermined ordered structure as precursor templates to induce the self-assembly of egg white-derived peptides (EWDP) to generate stable spherical architectures for the enhancement of curcumin (Cur). The resulting Z-EWDP-HA NPs encapsulated hydrophobic Cur through robust hydrogen bonding and hydrophobic interactions with high encapsulation efficiency (97.38% at pH 7.0). The NPs presented superior Cur aqueous solubility, redispersibility, and photothermal stability. More importantly, the self-assembled EWDP could exert synergistic antioxidant activity with Cur and enhance the bioaccessibility of Cur. Meanwhile, the favorable biocompatibility and membrane affinity of EWDP further prolonged residence and time-controlled release feature of Cur in the small intestine. Precursor template-induced multicomponent peptides' self-assembly provides an efficient and controllable strategy for co-enhanced bioactivity and self-assembly capacity of peptides, which could dramatically broaden the functionalization of multicomponent peptides hydrolyzed from natural food proteins.