摘要
采用荧光光谱法、紫外光谱法和圆二色光谱法并结合电化学方法,研究了大黄酸铜配合物与牛血清白蛋白之间的相互作用.结果表明,大黄酸铜配合物能显著猝灭牛血清白蛋白的内源荧光并以静态猝灭为主;计算了298和309 K温度下的结合常数和结合位点,热力学参数和大黄酸铜配合物的电化学行为说明大黄酸铜配合物与牛血清白蛋白之间具有较强的疏水作用力;依据F rster的偶极-偶极非辐射能量转移理论,计算出大黄酸铜在蛋白质中的结合位置与色氨酸残基间的距离为3.21 nm,表明大黄酸铜的部分片段能够插入蛋白质分子内部;探讨了大黄酸铜配合物对牛血清白蛋白构象的影响.
The interaction between Rhein-Cu and bovine serum albumin（BSA） was investigated by fluorescence,ultraviolet and circular dichroism spectra in conjunction with electrochemical methods.The results indicate that Rhein-Cu leads to the intrinsic fluorescence quenching of BSA through a static quenching procedure.The binding constants K and binding site n at 298 and 309 K were obtained.The binding locality was found to be an area of 3.21 nm away from tryptophan residue in BSA based on Frster non-radiation energy transfer mechanism.The experimental results show that Rhein-Cu can be inserted into the BSA,quenching the inner fluorescence by forming Rhein-Cu/BSA complex.The binding power between Rhein-Cu and BSA is mainly hydrophobic interaction according to the thermodynamic parameters and the electrochemical behaviors of Rhein-Cu.The effect of Rhein-Cu on the conformation of BSA was also analyzed.
出处
《高等学校化学学报》
SCIE
EI
CAS
CSCD
北大核心
2011年第6期1277-1283,共7页
Chemical Journal of Chinese Universities
基金
国家自然科学基金(批准号:20961009)资助
关键词
大黄酸铜
牛血清白蛋白
荧光光谱
紫外光谱
圆二色光谱
Rhein-Cu
Bovine serum albumin（BSA）
Fluorescence spectrum
Ultraviolet spectrum
Circular dichroism spectrum
