GLPGPSGEEGKR: Fe2+ chelating characterization and potential transport pathways for improving Fe2+ bioavailability in Caco-2 cells
文献类型： 外文期刊
作者： Lin, Shanting 1 ; Hu, Xiao 1 ; Yang, Xianqing 1 ; Chen, Shengjun 1 ; Wu, Yanyan 1 ; Hao, Shuxian 1 ; Huang, Hui 1 ; Li, Laihao 1 ;
作者机构： 1.Chinese Acad Fishery Sci, South China Sea Fisheries Res Inst, Key Lab Aquat Prod Proc, Minist Agr & Rural, 231 West Xingang Rd, Guangzhou 510300, Peoples R China
2.Jiangsu Ocean Univ, Coinnovat Ctr Jiangsu Marine Bioind Technol, Lianyungang 222005, Peoples R China
3.Collaborat Innovat Ctr Prov & Ministerial Coconst, Dalian 116034, Peoples R China
关键词： Fe2+ chelating peptide; Peptide-G-R-Fe2+ complex; Chelating properties; Bioavailability; Transport mechanism
期刊名称：FOOD BIOSCIENCE （ 影响因子：5.318； 五年影响因子：5.846 ）
ISSN： 2212-4292
年卷期： 2022 年 48 卷
页码：
收录情况： SCI
摘要： We investigated the Fe2+ chelating properties and the mechanism of improving Fe2+ bioavailability of the Fe2+ chelating peptide (GLPGPSGEEGKR, peptide-G-R). Fe2+ was chelated with the carboxyl oxygen atom of the GluGlu residue in the form of monodentate and bidentate chelating mode. After chelation, peptide-G-R was folded and aggregated to form spherical particles with increasing particle size. Peptide-G-R could increase the Fe2+ transport/retention/uptake rate and the relative expression levels of divalent metal transporter 1 (DMT1) in the Caco-2 cells monolayer model. Peptide-G-R could reverse the inhibition of phytic acid on the Fe2+ utilization in the Caco-2 cells monolayer model. Molecular dynamics simulation showed that peptide-G-R interacted with DMT1 in the form of intermolecular hydrogen bonds. The transport mechanism of the peptide-G-R-Fe2+ complex included endocytosis (main pathway), paracellular pathway (auxiliary way), and DMT1 (potential pathway). Thus, peptide-G-R derived from tilapia skin collagen could be used as a dietary iron supplement.
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