Supramolecular protein-peptide co-assembly mediated by Ca2+enhances curcumin penetration through intestinal barriers

文献类型： 外文期刊

第一作者： Tian, Longjiang

作者： Tian, Longjiang;Zhao, Yiheng;Ren, Wenshuo;Yang, Meng;Li, Yajuan;Li, Shanglin;Yu, Yiding;Zhang, Ting;Du, Zhiyang;Tian, Longjiang;Zhao, Yiheng;Ren, Wenshuo;Yang, Meng;Li, Yajuan;Li, Shanglin;Yu, Yiding;Zhang, Ting;Du, Zhiyang;Pan, Fei;Yu, Yiding

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关键词： Protein-peptide co-assembly; Calcium ion; Mucus permeation; Curcumin; Bioavailability

期刊名称：FOOD HYDROCOLLOIDS （ 影响因子：12.4； 五年影响因子：13.3 ）

ISSN： 0268-005X

年卷期： 2025 年 169 卷

页码：

收录情况： SCI

摘要： The size-tunable protein-peptide co-assembly strategy has provided novel insights into the design of highbioavailability delivery vehicles. This study involved a calcium ion (Ca2+)-mediated co-assembly (CA) of casein (CN) and egg white peptide (EWP) to encapsulate the model hydrophobic curcumin (Cur), denoted as EWP-Ca2+-CN-Cur. The findings reveal that Ca2+ acts as a pivotal orchestrator in modulating the microscopic interaction patterns of co-assembly, inducing non-covalent interaction reconstruction through entropy-enthalpy co-mediated effects to drive assembly processes while triggering intra-assembly cross-beta sheets compaction. The resulting ultrasmall nanospheres (63 +/- 0.40 nm) achieved concurrent optimization of guest molecule encapsulation capacity and stability enhancement. More importantly, EWP-Ca2+-CN-Cur exhibits remarkable enhancement in Cur internalization in Caco-2 cells, alongside excellent mucus penetration, epithelial absorption, and transport efficiency. It also demonstrates intestinal sustained-release properties and potential antiinflammatory effects. We anticipate that this Ca2+-mediated protein-peptide co-assembly strategy could provide a facile approach for the design of biocompatible oral delivery systems and the enhancement of bioavailability for hydrophobic components.

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