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PHOTOINDUCED DEGRADATION AND MODIFICATION OF PHOTOFRIN II IN CELLS in vitro
Author(s) -
Moan Johan,
Rimington Claude,
Malik Zvi
Publication year - 1988
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1988.tb02738.x
Subject(s) - porphyrin , photochemistry , fluorescence , chemistry , degradation (telecommunications) , biophysics , absorption (acoustics) , in vitro , biochemistry , materials science , biology , optics , telecommunications , physics , computer science , composite material
— Human cells of the line NHIK 3025 were incubated with Photofrin II (PII) and exposed to light. Fluorescence‐ and absorption spectra of PII in the cells were measured. Light exposure resulted in a degradation of PII in the cells and changes in the shape of the fluorescence spectra. These changes are probably partly due to a photochemical modification of PII and to a relocalization of PII in the cells. Notably, a destruction of binding sites for PII on or close to proteins was caused by the light exposure. The rate of the light‐induced decay of the porphyrin fluorescence intensity was only slightly increasing with the PII concentration, indicating that each porphyrin molecule is mainly degraded by photoproducts originating from itself. On the other hand, the rate of the degradation of porphyrin binding sites on the proteins increased with increasing PII concentrations. The excitation spectrum of PII in cells has a peak at285–290 nm attributed to energy transfer from proteins to porphyrins located close to the proteins. The intensity of this peak relative to the intensity of the Soret band increases with decreasing porphyrin concentrations. This might indicate that some of the binding sites close to proteins have a higher affinity for the porphyrin than binding sites at longer distances from the proteins.