Collagen-derived Fe2+-chelating peptide: Key amino acids for Fe2+chelating and mechanisms for enhancing cellular Fe2+bioavailability

文献类型： 外文期刊

第一作者： Li, Jun

作者： Li, Jun;Lin, Shanting;Lin, Shanting;Chen, Shengjun;Hu, Xiao;Lin, Shanting;Li, Zhenxing

作者机构：

关键词： Fe 2+-chelating peptide; Key amino acids; Fe 2+chelating mode; Characterization; Cellular transport mechanism

期刊名称：FOOD CHEMISTRY （ 影响因子：9.8； 五年影响因子：9.7 ）

ISSN： 0308-8146

年卷期： 2025 年 493 卷

页码：

收录情况： SCI

摘要： This study aimed to identify the key amino acids and modes for chelation between peptides and Fe2+, characterize the structural and morphological differences, and explore the mechanisms by which peptide-Fe2+ complexes enhanced cellular Fe2+ bioavailability. The results demonstrated that the -Glu-Glu- motif played a crucial role in Fe2+ chelation, adopting bidentate or multidentate chelating mode. Interestingly, although the C-terminal hydrophobic residues (Gly, Leu, Hyp, Pro) didn't directly chelate with Fe2+, they played an essential role in stabilizing the peptide conformation. Moreover, peptides and peptide-Fe2+ complexes exhibited different structures and morphologies. Additionally, peptide-Fe2+ complexes significantly enhanced cellular Fe2+ transport/retention/utilization rate, increased intracellular ferritin levels, and modulated the expression of DMT1, PCBP2, and FPN1 proteins. The improvement of Fe2+ transport by peptide-Fe2+ complexes was mediated through multiple pathways including endocytosis, paracellular pathway, and DMT1. These findings can provide valuable insights for the development of Fe2+-chelating peptides as potential dietary iron supplements.

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