GLPGPSGEEGKR: Fe2+ chelating characterization and potential transport pathways for improving Fe2+ bioavailability in Caco-2 cells. (August 2022)

• Record Type: Journal Article
• Authors: Lin, Shanting; Hu, Xiao; Yang, Xianqing; Chen, Shengjun; Wu, Yanyan; Hao, Shuxian; Huang, Hui; Li, Laihao
• Is Part Of: Food bioscience. Volume 48(2022)
• Publication Date: 2022-08
• Subjects: Fe2+ chelating peptide -- Peptide-G-R-Fe2+ complex -- Chelating properties -- Bioavailability -- Transport mechanism; BPDS Bathophenanthroline disulfonic acid -- CD circular dichroism -- CCK-8 Cell Counting Kit-8 -- CPP caseinophosphopeptide -- DMT1 divalent metal transporter 1 -- DPs duck egg white peptides -- EDTA Ethylene Diamine Tetraacetic Acid -- FTIR Fourier transform infrared -- HEPES 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid -- MEM minimum essential medium -- PDB protein data bank -- RT-PCR reverse transcription-polymerase chain reaction -- RIPA radio immunoprecipitation assay -- SEM scanning electron microscope -- UV–Vis ultraviolet–visible; Food -- Biotechnology -- Periodicals; Food -- Research -- Periodicals; Aliments -- Biotecnologia -- Revistes; Aliments -- Investigació -- Revistes; Food -- Biotechnology; Food -- Research; Revistes electròniques; Periodicals; 664.005
• DOI: 10.1016/j.fbio.2022.101806
• Languages: English
• ISSNs: 2212-4292

Abstract

Abstract: We investigated the Fe 2+ chelating properties and the mechanism of improving Fe 2+ bioavailability of the Fe 2+ chelating peptide (GLPGPSGEEGKR, peptide-G-R). Fe 2+ was chelated with the carboxyl oxygen atom of the Glu-Glu 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 Fe 2+ 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 Fe 2+ 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-Fe 2+ 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. Graphical abstract: Image 1 Highlights: Fe 2+ chelated with oxygen atom of Glu-Glu residue in the peptide-G-R in a form of monodentate and bidentate chelating mode. Peptide-G-R was folded and aggregated to form spherical particles with increased particle size after chelated with Fe 2+ . Peptide-G-R could increase the bioavailability of Fe 2+ and reverse the inhibition of phytic acid on the Fe 2+ utilization in Caco-2 cells. The transport mechanism of peptide-G-R-Fe 2+ complex may include endocytosis, paracellular pathway and DMT1.