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

被引:15
|
作者
Li, Yajuan
Liu, Jingbo
Shi, Xiaoxia
Zhang, Hui
Zhang, Leiyi
Xu, Ziang
Zhang, Ting
Yu, Yiding
Du, Zhiyang [1 ]
机构
[1] Jilin Univ, Jilin Prov Key Lab Nutr & Funct Food, Changchun 130062, Peoples R China
基金
中国国家自然科学基金;
关键词
Multicomponent peptides; Self-assembly; Curcumin; Precursor template; Biodistribution; NANOPARTICLES;
D O I
10.1016/j.foodres.2023.113120
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
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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页数:11
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