Photophysical studies on the binding of tetrasulfonatophenylporphyrin to lens proteins.
Previous studies have shown that mesotetra(p-sulfonatophenyl)porphine (TPPS) binds to lens proteins. This characteristic should increase the residence time of the sensitizer in the lens and therefore enhance the probability of inducing photooxidative damage to that tissue in vivo. Subsequent in vivo studies have verified that contention. The present studies were performed to determine the effect of such binding on the spectroscopy and photophysics of the porphyrins. It was found that the binding of TPPS (1) quenches the fluorescence of lens proteins, (2) causes a shift in the ground state absorption spectra, fluorescence excitation spectra and the triplet excited state spectrum of TPPS to longer wavelengths and (3) results in an increase in the triplet state lifetime of TPPS. In the presence of the isolated crystallins the average triplet lifetime increases in the following order: gamma less than beta less than alpha.
Roberts
J E
JE
Fordham University, New York, NY 10023.
Atherton
S J
SJ
Dillon
J
J
D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003459:Crystallins / Q000737:chemistry / Q000378:metabolism*; D066298:In Vitro Techniques; D010777:Photochemistry; D011166:Porphyrins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D013050:Spectrometry, Fluorescence; D014578:Uroporphyrins / Q000378:metabolism
D003459:Crystallins; D011166:Porphyrins; D014578:Uroporphyrins; C016136:tetraphenylporphine sulfonate