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Biophys J, February 2001, p. 801-811, Vol. 80, No. 2
and
*Department of Physiology and Biophysics and the Program in
Macromolecular Structure, University of California at Irvine,
Irvine, California 92697-4560 USA and Department of
Biochemistry, School of Medical Sciences, University of Bristol,
Bristol, BS8 1TD, United Kingdom
Melittin is arguably the most widely studied amphipathic,
membrane-lytic 
-helical peptide. Although several lines of evidence suggest an interfacial membrane location at low concentrations, melittin's exact position and depth of penetration into the
hydrocarbon core are unknown. Furthermore, the structural basis for its
lytic action remains largely a matter of conjecture. Using a novel
x-ray absolute-scale refinement method, we have now determined the
location, orientation, and likely conformation of monomeric melittin in oriented phosphocholine lipid multilayers. Its helical axis is aligned
parallel to the bilayer plane at the depth of the glycerol groups, but
its average conformation differs from the crystallographic structure.
As observed earlier for another amphipathic -helical peptide, the
lipid perturbations induced by melittin are remarkably modest. Small
bilayer perturbations thus appear to be a general feature of
amphipathic helices at low concentrations. In contrast, a dimeric form
of melittin causes larger structural perturbations under otherwise
identical conditions. These results provide direct structural evidence
that self-association of amphipathic helices may be the crucial initial
step toward membrane lysis.
Biophys J, February 2001, p. 801-811, Vol. 80, No. 2
© 2001 by the Biophysical Society 0006-3495/01/02/801/11 $2.00
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