4.7 Article

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

Journal

FOOD RESEARCH INTERNATIONAL
Volume 172, Issue -, Pages -

Publisher

ELSEVIER
DOI: 10.1016/j.foodres.2023.113120

Keywords

Multicomponent peptides; Self-assembly; Curcumin; Precursor template; Biodistribution

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In this study, zein-hyaluronic acid nanoparticles were used as templates to induce the self-assembly of egg white-derived peptides for the enhancement of curcumin. The resulting nanoparticles showed high encapsulation efficiency and improved solubility and stability of curcumin. The self-assembled peptides exhibited synergistic antioxidant activity with curcumin and enhanced its bioaccessibility.
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 selfassembly 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 selfassembled 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.

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