Investigation on the interaction of pyrene with bovine serum albumin using spectroscopic methods.
Investigation on the interaction of pyrene with bovine serum albumin using spectroscopic methods.
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DOI：
10.1016/j.saa.2014.01.132
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发表时间：
2014-05
期刊：
影响因子：
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通讯作者：
C. Xu;J. Gu;Xiping Ma;Tian Dong;X. Meng
中科院分区：
文献类型：
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作者：
C. Xu;J. Gu;Xiping Ma;Tian Dong;X. Meng
用光谱学方法研究了在生理条件下芘与牛血清白蛋白(BSA)的相互作用。发射猝灭的光谱分析表明，Py对BSA的猝灭机理是静态的。结果表明，298K时，芘-牛血清白蛋白络合物的结合位点数为1.2×10~6L·−~(-1)，结合常数为2.63×10~6L·mol~(-1)。焓变(ΔH)和熵变(ΔS)表明，范德华作用力和氢键稳定了芘-牛血清白蛋白络合物。通过荧光共振能量转移(FRET)机制，确定了色氨酸与芘之间的能量转移距离(r=272 nm)。同步荧光光谱、三维荧光光谱和圆二色谱结果表明，Py诱导了BSA的构象变化。
This paper was designed to investigate the interaction of pyrene with bovine serum albumin (BSA) under physiological condition by spectroscopic methods. Spectroscopic analysis of the emission quenching revealed that the quenching mechanism of BSA by pyrene was static. The binding sites and constants of pyrene–BSA complex were observed to be 1.20 and 2.63 × 106L mol−1at 298 K, respectively. The enthalpy change (ΔH) and entropy change (ΔS) revealed that van der Waals forces and hydrogen bonds stabilized the pyrene–BSA complex. Energy transfer from tryptophan to pyrene occurred by a FRET (fluorescence resonance energy transfer) mechanism, and the distance (r= 2.72 nm) had been determined. The results of synchronous, three-dimensional fluorescence, and circular dichroism spectra showed that the pyrene induced conformational changes of BSA.