Zervamicins, a structurally characterised peptide model for membrane ion channels
References (29)
Neuron
(1989)Neuron
(1989)- et al.
Biophys. J.
(1984) - et al.
FEBS Lett.
(1983) - et al.
Biophys. J.
(1983) - et al.
Biochim Biophys. Acta
(1988) - et al.
FEBS Lett.
(1990) J. Mol. Biol.
(1991)- et al.
Biochem. Biophys. Res. Commun.
(1991) - et al.
FEBS Lett.
(1991)
Science
Prog. Biophys. Mol. Biol.
Mol. Cell. Biochem.
Cited by (23)
Interaction of zervamicin IIB with lipid bilayers. Molecular dynamics study
2011, Computational Biology and ChemistryCitation Excerpt :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.
Membrane association and activity of 15/16-membered peptide antibiotics: Zervamicin IIB, ampullosporin A and antiamoebin I
2005, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :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 - BiomembranesCitation Excerpt :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].
NMR structure of the channel-former zervamicin IIB in isotropic solvents
2000, FEBS LettersNon-standard amino acids in peptide design and protein engineering
1992, Current Opinion in Structural Biology
- +
Present address: Laboratory of Molecular Biophysics, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K.