Co-Authors:
Rosenthal, I., Department of Food Science, Volcani Institute, P.O. Box 6, Bet Dagan, 50250, Israel
Shafirovich, V.Y., Chemistry Department and Radiation, Solid State Laboratory, New York University, New York, New York, 10003, United States
Geacintov, N.E., Chemistry Department and Radiation, Solid State Laboratory, New York University, New York, New York, 10003, United States
Ben‐Hur, E., New York Blood Center, 310 E. 67th St, New York, New York, 10021, United States
Horowitz, B., New York Blood Center, 310 E. 67th St, New York, New York, 10021, United States
Abstract:
Abstract Fluoride is known to inhibit the photodynamic activity of aluminum phthalocyanine in a variety of biological systems. In order to gain insight into this phenomenon, the effect of fluoride on the photophysical properties of free and albumin‐bound chloroaluminum phthalocyanine sulfonate (AlPcSn.) were studied. The association constant of NaF with AlPcSn, in aqueous solution was measured as 500 ± 20 M−1. This binding affects the photophysical properties of the dye: the absorption bands in the visible range are blue‐shifted by 6–8 nm, and this effect is mirrored in the fluorescence emission spectrum. Human serum albumin significantly quenched the dye fluorescence independent of the presence of fluoride ion. The transient absorption spectrum of the excited dye triplet is unchanged by NaF, but the quantum yield for its generation is increased by 50%, with no decrease in its lifetime. Formation of fluoroaluminum phthalocyanine complexes was also observed in tetrabutylammonium fluoride‐assisted solutions in wet acetonitrile. The fluoro‐AlPcSn, complex is a better photosensitizer for generation of singlet oxygen than the original dye‐hydroxyl ion complex, as confirmed using the imidazole‐N,N‐dimethyl‐4‐nitrosoaniline method. On the other band, the fluoro‐AlPcSn. complex exhibits an intense inhibitory effect on photohemolysis of red blood cells (RBC) even after the cells are washed to remove free dye and fluoride prior to irradiation, indicating that once the dye is attached to the cellular site, the fluoride ligand is no longer prone to displacement (by hydroxyl ion, for example). Nonetheless, it is clear from the spectroscopic data that the new fluoro complex is an efficient sensitizer for photo‐oxidation. Therefore, the reduced photodynamic action of the fluoro‐AlPcSn. complex on RBC (Ben‐Hur et al., Photochem. Photobiol. 58, 351–355, 1993) may result from a lowering of the efficiency of interaction of the fluorodye complex with sensitive cell target moieties. Copyright © 1994, Wiley Blackwell. All rights reserved
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