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J. Biol. Chem., Vol. 265, Issue 33, 20202-20209, Nov, 1990
Y Shai, D Bach and A Yanovsky
Six analogues of teh 33-residue shark repellent neurotoxin pardaxin were
synthesized by the solid phase method: [Ala13]pardaxin,
[Gly14,Gly15]pardaxin, des[1----9]pardaxin, [N1-succinamido]pardaxin,
C33-dihydroxyethylamido]pardaxin, and C33-[diaminoethylamido]pardaxin. The
spectroscopic and functional characterizations of the analogues are
described. The peptides were characterized spectroscopically by circular
dichroism (CD) before and after binding to soybean vesicles. They were
characterized functionally by measuring their potential to evoke the
dissipation of diffusion potential and calcein release from sonicated
unilamellar soybean liposomes, by determining their ability to create
single channels in planar bilayers, and by measuring their cytolytic
activity on human erythrocytes. The behavior of the analogues modified at
the C terminus is similar to that of pardaxin. [N'- succinamido]Pardaxin,
however, reveals an increase in alpha-helicity both alone and in the
presence of liposomes. It has the same potency as pardaxin to dissipate
diffusion potential, to evoke calcein release and to produce single
channels in lipid bilayers, but at a slower rate than that of pardaxin. It
has more than 70-fold less cytolytic activity than pardaxin. [Ala13]
Pardaxin has twice the alpha-helical content than pardaxin, both alone and
in the presence of vesicles, yet it has less effect on the diffusion
potential and calcein release, and it does not have cytolytic activity on
human erythrocytes. Both [Gly14,Gly15]pardaxin and des[1----9]pardaxin are
much less potent than pardaxin in all effects. However des[1----9]pardaxin
exhibits a slight change in alpha-helicity upon binding to vesicles,
whereas [Gly14,Gly15]pardaxin does not. The results support a model in
which pardaxin is composed of two putative alpha-helices separated by
proline. The N-terminal alpha-helix is important for the insertion of the
peptide to the lipid bilayer, and the C-terminal amphiphilic alpha- helix
is the ion channel lining segment of pardaxin.
Channel formation properties of synthetic pardaxin and analogues
Department of Membrane Research, Weizmann Institute of Science, Rehovot, Israel.
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