摘要
采用荧光和紫外光谱法研究了邻苯二酚同牛血清白蛋白(BSA)的作用。邻苯二酚对BSA内源荧光猝灭机理为静态猝灭,两者之间生成了不发荧光的复合物。根据双对数方程计算了复合物的结合常数KA和结合位点数n。确定邻苯二酚与BSA只有一个结合位点(可能位于Site I)。通过热力学参数得出邻苯二酚与BSA之间主要作用力是疏水作用。同步荧光的结果表明邻苯二酚改变了BSA的分子构象,使色氨酸残基的极性增加,酪氨酸残基的疏水性增强。
The interaction of o-dibydroxybenzene with bovine serum albumin （BSA） was investigated by fluorescence and absorption spectroscopy. The quenching mechanism belongs to static quenching. BSA had reacted with o-dihydroxybenzene and formed a new nonflurorescence complex.The binding constants and the number of bonding sites were obtained by double-log regression equation. There was only one binding site （ possibly site Ⅰ）for binding of o-dihydroxybenzene with BSA. Thennodynamic parameters indicated that the hydrophobic forces played a major role in the binding of o-dihydroxybenzene to BSA. The conformation of BSA has been changed by means of synchronous fluorescence in the presence of o-Dihydroxybenzene, resulting in the increase of the polarity around tryptophan residues and the increase of the hydrophobicity of the tyrosine residues.
出处
《化学研究与应用》
CAS
CSCD
北大核心
2009年第2期155-158,共4页
Chemical Research and Application
基金
辽宁省教育厅基金资助项目(20060687)
作者简介
联系人简介：臧树良（1951-），男，教授,博士生导师，研究方向有机有毒小分子和生物大分子的相互作用。Email：dalin0417@163．com
