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• W2012593935 abstract "The synthetic peptide (C(18)H(37))(2)NCOCH(2)OCH(2)CON-(Gly)(3)-Pro-(Gly)(3)-OCH(2)Ph forms chloride-selective channels in liposomes and exhibits voltage-gating properties in planar phospholipid bilayers. The peptide fragment of the channel is based on a conserved motif in naturally occurring chloride transporters. Membrane-anchoring residues at the N- and C-terminal ends augment the peptide. NMR spectra (1D and 2D) of the channel in CDCl(3) showed significant variation in the absence and presence of stoichiometric tetrabutylammonium chloride (Bu(4)NCl). One-dimensional solution-state NMR titration studies combined with computational molecular simulation studies indicate that the peptide interacts with the salt as an ion pair and H-bonds chloride. To our knowledge, this is the first structural analysis of any synthetic anion-channel salt complex." @default.
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• W2012593935 date "2006-01-12" @default.
• W2012593935 modified "2023-09-23" @default.
• W2012593935 title "NMR Structure and Dynamic Studies of an Anion-Binding, Channel-Forming Heptapeptide" @default.
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• W2012593935 doi "https://doi.org/10.1021/ja055887j" @default.
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