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Photobinding of carprofen to protein

Moser, 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.

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  • Photobinding of carprofen to protein

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DOI

  • J Moser
  • F Bosca
  • WW Lovell
  • JV Castell
  • MA Miranda
  • A Hye

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.

Original languageEnglish
Pages (from-to)13-19
Number of pages7
JournalJournal of photochemistry and photobiology b-Biology
Volume58
Issue number1
Publication statusPublished - Oct-2000

    Keywords

  • albumin, carbazole, carprofen, dehalogenation, fluorescence, photobinding, photolysis, ANTIINFLAMMATORY DRUGS, TIAPROFENIC ACID, PHOTOTOXICITY, INVITRO, DERMATITIS, MECHANISM, BINDING, ALBUMIN

ID: 32266004