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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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Bibliographic Details
Published in:Journal of photochemistry and photobiology. B, Biology Biology, 2005-09, Vol.80 (3), p.235-242
Main Authors: Hu, Yan-Jun, Liu, Yi, Jiang, Wei, Zhao, Ru-Ming, Qu, Song-Sheng
Format: Article
Language:English
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Summary: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.
ISSN:1011-1344
1873-2682
DOI:10.1016/j.jphotobiol.2005.04.005