Zervamicins, a structurally characterised peptide model for membrane ion channels

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Voltage dependent membrane channels are formed by the zervamicins, a group of α-aminoisobutyric acid containing peptides. The role of polar residues like Thr, Gln and Hyp in promoting helical bundle formation is established by dramatically reduced channel lifetimes for a synthetic apolar analog. Crystal structures of Leu1-zervamicin reveal association of bent helices. Polar contacts between convex faces result in an ‘hour glass’ like arrangement of an aqueous channel with a central constriction. The structure suggests that gating mechanisms may involve movement of the Gln11 carboxamide group. Gln3 may play a role in modulating the size of the channel mouth.

References (29)

  • UnwinN.

    Neuron

    (1989)
  • MillerC.

    Neuron

    (1989)
  • HallJ.E. et al.

    Biophys. J.

    (1984)
  • MathewM.K. et al.

    FEBS Lett.

    (1983)
  • CoronadoR. et al.

    Biophys. J.

    (1983)
  • MellorI.R. et al.

    Biochim Biophys. Acta

    (1988)
  • WoolfsonD.N. et al.

    FEBS Lett.

    (1990)
  • Von HeijneG.

    J. Mol. Biol.

    (1991)
  • WoolfsonD.N. et al.

    Biochem. Biophys. Res. Commun.

    (1991)
  • DempseyC.E. et al.

    FEBS Lett.

    (1991)
  • LearJ.D. et al.

    Science

    (1988)
  • MontalM. et al.
  • SansomM.S.P.

    Prog. Biophys. Mol. Biol.

    (1991)
  • MathewM.K. et al.

    Mol. Cell. Biochem.

    (1983)
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      But the conventional model for voltage-gated peptaibol channel action involves the formation of the water-filled pore by a bundle of parallel helices (Laver, 1994). Different conductance levels are thought to correspond to different numbers of helices in a bundle (Agarwalla et al., 1992). According to barrel-stave model (BS-model) of peptaibol action, peptaibol adsorbs on the membrane surface and embeds into the lipid bilayer under the transmembrane potential.

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      Well-defined multilevel ion channels are formed by ZER in diphytanoyl PC membrane, which could be described by the barrel-stave model with N = 4–8 helices per bundle [13]. The single channel conductance induced by ZER was shown to be comparable with that of ALA for similar experimental conditions [12]. Channel formation appears to be voltage-dependent with activation by a cis-positive membrane potential [3,13].

    • Ion transport across a phospholipid membrane mediated by the peptide trichogin GA IV

      2002, Biochimica et Biophysica Acta - Biomembranes
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      Zervamicins belong to another family of peptaibols, i.e. 16-residue antibiotic peptides isolated from Emericellopsis salmosynnemata[7]. The major component of the zervamicin analogues, zervamicin IIB (Table 1), shows almost the same ion conducting properties as alamethicin [8,9]. The voltage-induced conductance is asymmetric with a higher current observed at cis-positive potentials compared to that at a cis-negative voltage [4,5,9,10].

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    Present address: Laboratory of Molecular Biophysics, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K.

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