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• W2078385435 abstract "Divalent-metal transporter 1 (DMT1) is involved in the intestinal iron absorption and in iron transport in the transferrin cycle. It transports metal ions at low pH (≈5.5), but not at high pH (7.4), and the transport is a proton-coupled process. Previously it has been shown that transmembrane domain 4 (TM4) is crucial for the function of this protein. Here we provide the first direct experimental evidence for secondary-structural features and membrane insertions of a 24-residue peptide, corresponding to TM4 of DMT1 (DMTI-TM4), in various membrane-mimicking environments by the combined use of CD and NMR spectroscopies. The peptide mainly adopts an α-helical structure in trifluoroethanol, SDS and dodecylphosphocholine micelles, and dimyristoyl phosphatidylcholine and dimyristoyl phosphatidylglycerol small unilamellar vesicles. It has been demonstrated from both Hα secondary shifts and nuclear-Overhauser-enhancement (NOE) connectivities that the peptide is well folded into an α-helix from Val8 to Lys23 in SDS micelles at pH 4.0, whereas the N-terminus is highly flexible. The α-helical content estimated from NMR data is in agreement with that extracted from CD simulations. The highest helicity was observed in the anionic phospholipids {1,2-dimyristoyl-sn-glycero-3-[phospho-rac-(1-glycerol)]}, indicating that electrostatic attraction is important for peptide binding and insertion into the membranes. The secondary-structural transition of the peptide occurred at pH 4.3 in the 2,2,2-trifluoroethanol (TFE) water mixed solvent, whereas at a higher pH value (5.6) in SDS micelles, DMT1-TM4 exhibited a more stable structure in SDS micelles than that in TFE in terms of changing the pH and temperature. PAGE did not show high-molecular-mass aggregates in SDS micelles. The position of the peptide relative to SDS micelles was probed by the effects of 5- and 16-doxylstearic acids on the intensities of the peptide proton resonances. The results showed that the majority of the peptide is inserted into the hydrophobic interior of SDS micelles, whereas the C-terminal residues are surface-exposed. The ability of DMT1-TM4 to assume transmembrane features may be crucial for its biological function in vivo." @default.
• W2078385435 created "2016-06-24" @default.
• W2078385435 creator A5005228021 @default.
• W2078385435 creator A5031516698 @default.
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• W2078385435 date "2003-06-15" @default.
• W2078385435 modified "2023-10-18" @default.
• W2078385435 title "Membrane-inserted conformation of transmembrane domain 4 of divalent-metal transporter" @default.
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• W2078385435 doi "https://doi.org/10.1042/bj20030075" @default.
• W2078385435 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1223444" @default.
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• W2078385435 hasPublicationYear "2003" @default.
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