Photobinding of carprofen to proteinMoser, J., Bosca, F., Lovell, WW., Castell, JV., Miranda, MA. & Hye, A., Oct-2000, In : Journal of photochemistry and photobiology b-Biology. 58, 1, p. 13-19 7 p.
Research output: Contribution to journal › Article › Academic › peer-review
Carprofen is a non-steroidal antiinflammatory drug with marked photosensitising properties. In order to elucidate the mechanisms underlying the phenomenon of drug-protein photobinding, mixtures of the drug and human serum albumin were irradiated under different experimental conditions. After irradiation and subsequent gel-filtration chromatography of the photomixture, the eluting protein fraction was analysed by means of fluorescence spectroscopy. The formation of drug-protein photoadducts could be evidenced by the characteristic emission properties of the carbazole chromophore. The photobinding of the drug to human serum albumin appears to involve the formation of aryl radicals resulting from carbon-halogen photocleavage. This mechanistic interpretation is supported by the observed variations in the intensity of the fluorescence spectra, which can be correlated with the lower quantum yield emission of chlorocarbazoles as compared to non-halogenated analogues. The results from laser flash photolysis studies are also in agreement with this proposal. (C) 2000 Elsevier Science B.V, All rights reserved.
|Number of pages||7|
|Journal||Journal of photochemistry and photobiology b-Biology|
|Publication status||Published - Oct-2000|
- albumin, carbazole, carprofen, dehalogenation, fluorescence, photobinding, photolysis, ANTIINFLAMMATORY DRUGS, TIAPROFENIC ACID, PHOTOTOXICITY, INVITRO, DERMATITIS, MECHANISM, BINDING, ALBUMIN