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Biophys J, May 2000, p. 2572-2580, Vol. 78, No. 5

*A. N. Belozersky Institute of Physico-Chemical Biology,
Moscow State University, Moscow 119899, Russia, and
Martin-Luther-Universität, Medizinische
Fakultät, Institut für Medizinische Physik und Biophysik,
06097 Halle, Germany
The photodynamic activity of sulfonated aluminum
phthalocyanines (AlPcSn, 1
n
4) was found to correlate with their affinity
for membrane lipids. Adsorbing to the surface of large unilamellar
vesicles (LUVs), aluminum phthalocyanine disulfonate induced the
highest changes in their electrophoretic mobility. AlPcS2
was also most efficient in mediating photoinactivation of gramicidin
channels, as revealed by measurements of the electric current across
planar lipid bilayers. The increase in the degree of sulfonation of
phthalocyanine progressively reduced its affinity for the lipid bilayer
as well as its potency of sensitizing gramicidin channel
photoinactivation. The portion of photoinactivated gramicidin channels,
, increased with rising photosensitizer concentration up to some
optimum. The concentration at which
was at half-maximum amounted to
80 nM, 30 nM, 200 nM, and 2 µM for AlPcS1,
AlPcS2, AlPcS3, and AlPcS4,
respectively. At high concentrations
was found to decrease, which
was attributed to quenching of reactive oxygen species and
self-quenching of the photosensitizer triplet state by its ground
state. Fluoride anions were observed to inhibit both
AlPcSn (2
n
4)
binding to LUVs and sensitized photoinactivation of gramicidin
channels. It is concluded that photosensitizer binding to membrane
lipids is a prerequisite for the photodynamic inactivation of
gramicidin channels.
Biophys J, May 2000, p. 2572-2580, Vol. 78, No. 5
© 2000 by the Biophysical Society 0006-3495/00/05/2572/09 $2.00
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