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 ...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.展开更多
基金supported by the National Key R&D Program of China(2018YFD0901102)the Key-Area Research and Development Program of Guangdong Province(2020B020226005)+4 种基金the China Agriculture Research System of MOF and MARA(CARS-46)he National Natural Science Foundation of China(31301454)the Special Scientific Research Funds for Central Non-profit Institutes,Chinese Academy of Fishery Sciences(2020TD69)the Central Public-interest Scientific Institution Basal Research Funds,South China Sea Fisheries Research Institute,CAFS(2021SD06)the Pearl River S&T Nova Program of Guangzhou(201906010081).
文摘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.
