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Biophys J, February 2002, p. 762-771, Vol. 82, No. 2
and
*Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian
Academy of Sciences, 117997 Moscow, Russia, and
Leiden Institute of Chemistry, Gorlaeus Laboratories,
Leiden University, 2300 RA, Leiden, The Netherlands
Zervamicin IIB is a 16-amino acid peptaibol that forms
voltage-dependent ion channels with multilevel conductance states in planar lipid bilayers and vesicular systems. The spatial structure of
zervamicin IIB bound to dodecylphosphocholine micelles was studied by
nuclear magnetic resonance spectroscopy. The set of 20 structures
obtained has a bent helical conformation with a mean backbone root mean
square deviation value of ~0.2 Å and resembles the structure in
isotropic solvents (Balashova et al., 2000. NMR structure of the
channel-former zervamicin IIB in isotropic solvents. FEBS
Lett 466:333-336). The N-terminus represents an
-helix, whereas the C-terminal part has a mixed
310/
R hydrogen-bond pattern. In the
anisotropic micelle environment, the bending angle on Hyp10 (23°) is
smaller than that (47°) in isotropic solvents. In the NOESY
(Nuclear Overhauser Effect Spectroscopy) spectra, the characteristic attenuation of the peptide signals by 5- and 16-doxylstearate relaxation probes indicates a peripheral mode of the peptaibol binding
to the micelle with the N-terminus immersed slightly
deeper into micelle interior. Analysis of the surface hydrophobicity reveals that the zervamicin IIB helix is amphiphilic and well suited to
formation of a tetrameric transmembrane bundle, according to the
barrel-stave mechanism. The results are discussed in a context of
voltage-driven peptaibol insertion into membrane.
Biophys J, February 2002, p. 762-771, Vol. 82, No. 2
© 2002 by the Biophysical Society 0006-3495/02/02/762/10 $2.00
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