摘要
在模拟生理条件下,采用荧光光谱法研究十溴联苯醚(Deca-BDE)与牛血清白蛋白(BSA)的相互作用。结果表明:Deca-BDE对BSA的内源荧光有静态猝灭作用。Deca-BDE与BSA在277,298和310K的结合常数分别为1.92×105,1.97×105和2.16×105L/mol。Deca-BDE在BSA接近于色氨酸残基附近有2个结合位点。热力学参数表明,Deca-BDE与BSA相结合的主要驱动力是疏水作用力。与Deca-BDE结合后,BSA色氨酸残基附近肽键伸展程度增加,蛋白分子结构疏松。
The interaction between decabromodiphenyl ether （Deca-BDE） and bovine serum albumin （BSA） in physiological buffer was studied by fluorescence quenching technique.Results showed that Deca-BDE has strong quenching function for the intrinsic fluorescence of BSA through a static quenching procedure.The binding constants （K） of Deca-BDE with BSA obtained by fluorescence quenching method were calculated to be 1.92×105,1.97×105 and 2.16×105 L/mol at 277,298 and 310 K,respectively.The binding sites of Deca-BDE on BSA had two and both were near tryptophan sites.Thermodynamic parameters obtained from data at different temperatures showed that the binding of Deca-BDE to BSA involved hydrophobic bonds pre-dominantly.The result of synchronous fluorescence spectra showed that binding of Deca-BDE with BSA could induce conformational changes in BSA.
出处
《分析化学》
SCIE
EI
CAS
CSCD
北大核心
2010年第10期1479-1482,共4页
Chinese Journal of Analytical Chemistry
基金
国家重点基础研究发展计划"973"项目(No.2009CB421604)资助
关键词
十溴联苯醚
牛血清白蛋白
荧光光谱
Decabromodiphenyl ether
Bovine serum albumin
Fluorescence quenching
