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Biophys J, October 2000, p. 2002-2009, Vol. 79, No. 4
and
*Physics Department, Rice University, Houston, Texas 77251-1892;
and
Department of Medicine, UCLA School of Medicine,
Los Angeles, California 90095 USA
Membrane pores spontaneously formed by antimicrobial
peptides in membranes were crystallized for the first time by
manipulating the sample hydration and temperature. Neutron diffraction
shows that magainins and protegrins form stable pores in fully hydrated fluid membranes. At lower hydration levels or low temperature, the
membrane multilayers crystallize. In one crystalline phase, the pores
in each bilayer arrange in a regular hexagonal array and the bilayers
are stacked into a hexagonal ABC lattice, corresponding to the cubic
close-packed structure of spheres. In another crystalline phase, the
bilayers are modulated into the rippled multilamellae, corresponding to
a 2D monoclinic lattice. The phase diagrams are described.
Crystallization of the membrane pores provides possibilities for
diffraction studies that might provide useful information on the pore structures.
Biophys J, October 2000, p. 2002-2009, Vol. 79, No. 4
© 2000 by the Biophysical Society 0006-3495/00/10/2002/08 $2.00
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