Supramolecular protein-peptide co-assembly mediated by Ca2+enhances curcumin penetration through intestinal barriers
文献类型： 外文期刊
作者： Tian, Longjiang 1 ; Zhao, Yiheng 1 ; Pan, Fei 3 ; Ren, Wenshuo 1 ; Yang, Meng 1 ; Li, Yajuan 1 ; Li, Shanglin 1 ; Yu, Yiding 1 ; Zhang, Ting 1 ; Du, Zhiyang 1 ;
作者机构： 1.Jilin Univ, Jilin Prov Key Lab Nutr & Funct Food, Changchun 130062, Peoples R China
2.Jilin Univ, Coll Food Sci & Engn, Changchun 130062, Peoples R China
3.Chinese Acad Agr Sci, Inst Apicultural Res, State Key Lab Resource Insects, Beijing 100093, Peoples R China
4.Hainan Univ, Sch Food Sci & Engn, Haikou 570228, Peoples R China
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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