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《Environmental Science & Technology》 2009-01
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Interaction between Sodium Dodecylbenzene Sulfonate and Bovine Serum Albumin

LIANG Yan-qiu1, SUN Peng2, DENG Bin2, ZHAO Xue2, ZANG Shu-liang2(1.Department of Environment and Biology,Shenyang Institute of Chemical Technology,Shenyang 110142,China;2.School of Chemistry,Liaoning University,Shenyang 110036,China)  
Binding interaction between sodium dodecylbenzene sulfonate(SDBS)and bovine serum albumin(BSA)was studied by fluorescence and absorption spectroscopy in physiological conditions.Results showed that fluorescence of BSA was quenched by SDBS,and the quenching mechanism was static.Binding constants and thermodynamic parameters were obtained at different temperatures.Main binding force was hydrogen bonds and Van der waals.Results of synchronous fluorescence spectra indicated that conformation of BSA was changed and hydrophobicity near tryptophan residues were increased at the presence of SDBS.
【Fund】: 辽宁省教育厅项目(20060687)
【CateGory Index】: R114
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