Fluorometric investigation of the interaction of bovine serum albumin with surfactants and 6-mercaptopurine
Fluorescence quenching in solutions of bovine serum albumin has been investigated in the presence of 6-mercaptopurine and ionic surfactants. Spectroscopic analysis of the emission quenching at different temperatures revealed that the quenching mechanism of bovine serum albumin by 6-mercaptopurine wa...
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Veröffentlicht in: | Journal of photochemistry and photobiology. B, Biology Biology, 2005-09, Vol.80 (3), p.235-242 |
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Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Fluorescence quenching in solutions of bovine serum albumin has been investigated in the presence of 6-mercaptopurine and ionic surfactants. Spectroscopic analysis of the emission quenching at different temperatures revealed that the quenching mechanism of bovine serum albumin by 6-mercaptopurine was dynamic quenching mechanism. The Stern–Volmer quenching model has been successfully applied, and the activation energy of the interaction between 6-mercaptopurine and bovine serum albumin as much as 4.26 kJ mol
−1 was calculated. The distance
r between donor (bovine serum albumin) and acceptor (6-mercaptopurine) was obtained according to fluorescence resonance energy transfer (FRET). The result of synchronous fluorescence spectra shows that the conformation of bovine serum albumin has been changed at the present of 6-mercaptopurine. |
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ISSN: | 1011-1344 1873-2682 |
DOI: | 10.1016/j.jphotobiol.2005.04.005 |