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J. Biol. Chem., Vol. 266, Issue 35, 23769-23775, 12, 1991
D Rapaport and Y Shai
Fluorescence measurements were used to monitor the interaction of the
neurotoxin pardaxin and its analogues with membranes. Eight peptides were
selectively labeled with the fluorophore 7-nitrobenz-2-oxa-1,3-
diazole-4-yl, either at their N-terminal or at their C-terminal. No
detectable changes in membrane permeability or hemolytic activity were
observed upon modification. Upon the titration of solutions containing the
different peptides with small unilamellar vesicles, the fluorescent
emission spectra of 7-nitrobenz-2-oxa-1,3-diazole-4-yl-labeled pardaxin and
its analogues, but not those of control peptides, displayed blue shifts in
addition to enhanced intensities upon relocation of the probe to a more
apolar environment. The results revealed that the N terminus of pardaxin is
buried within the lipid bilayer while the C terminus is located at the
bilayer's surface. Binding isotherms were obtained from the observed
increases in the fluorescence emission yields, from which surface partition
constants, in the range of 10(4) M-1, were in turn derived. The existence
of an aggregation process was suggested by the shape of the binding
isotherms. Furthermore, the results show good correlation between the
incidence of aggregation and the ability of the different analogues to
induce the release of relatively large molecules from vesicles. As such,
our results suggest that the mechanism of pore formation employed by
pardaxin and its analogues could be described by the "barrel stave" model.
Interaction of fluorescently labeled pardaxin and its analogues with lipid bilayers
Department of Membrane Research and Biophysics, Weizmann Institute of Science, Rehovot, Israel.
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