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

Food Res Int. 2023 Oct:172:113120. doi: 10.1016/j.foodres.2023.113120. Epub 2023 Jun 12.

Abstract

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.

Keywords: Biodistribution; Curcumin; Multicomponent peptides; Precursor template; Self-assembly.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biological Availability
  • Curcumin*
  • Egg White
  • Hydrogen Bonding
  • Peptides

Substances

  • Curcumin
  • Peptides