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Biophys J, June 1998, p. 2918-2925, Vol. 74, No. 6
*Monell Chemical Senses Center, Philadelphia, Pennsylvania
19104-3308 USA;
#Institute of Cytology of the Russian
Academy of Sciences, St. Petersburg 194064, Russia;
§National Institutes of Health, NICHD, Laboratory of
Physical and Structural Biology, 5/405, Bethesda, Maryland 20892 USA;
¶St. Petersburg Nuclear Physics Institute of the Russian
Academy of Sciences, Gatchina 188350, Russia;
Utah State
University, Logan, Utah 84322-5305 USA;
**University of Pennsylvania,
Philadelphia, Pennsylvania 19104 USA; and
##Veterans
Affairs Medical Center, Philadelphia, Pennsylvania 19104 USA
The cyclic lipodepsipeptide, syringomycin E, when
incorporated into planar lipid bilayer membranes, forms two types of
channels (small and large) that are different in conductance by a
factor of sixfold. To discriminate between a cluster organization-type channel structure and other possible different structures for the two
channel types, their ionic selectivity and pore size were determined.
Pore size was assessed using water-soluble polymers. Ion selectivity
was found to be essentially the same for both the small and large
channels. Their reversal (zero current) potentials with the sign
corresponding to anionic selectivity did not differ by more than 3 mV
at a twofold electrolyte gradient across the bilayer. Reduction in the
single-channel conductance induced by poly(ethylene glycol)s of
different molecular weights demonstrated that the aqueous pore sizes of
the small and large channels did not differ by more than 2% and were
close to 1 nm. Based on their virtually identical selectivity and size,
we conclude that large syringomycin E channels are clusters of small
ones exhibiting synchronous opening and closing.
Biophys J, June 1998, p. 2918-2925, Vol. 74, No. 6
© 1998 by the Biophysical Society 0006-3495/98/06/2918/08 $2.00
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