采用光谱和分子建模方法研究双酚 A 与牛血红蛋白的相互作用。
Interaction of bisphenol A with bovine hemoglobin using spectroscopic and molecular modeling methods.
机构信息
Shandong Key Laboratory of Water Pollution Control and Resource Reuse, School of Environmental Science and Engineering, Shandong University, China-America CRC for Environment and Health, Shandong Province, Jinan 250100, China.
出版信息
Appl Spectrosc. 2011 Nov;65(11):1250-3. doi: 10.1366/11-06357.
The interaction of bisphenol A with bovine hemoglobin (BHb) under physiological conditions was investigated by using fluorescence, ultraviolet-visible (UV-Vis) absorption, circular dichroism (CD), and molecular modeling. The experimental results showed that BPA can bind with BHb to form a complex. The binding constant Ka and the number of binding sites n were calculated to be 1.49 × 10(5) L mol(-1) and 1, respectively. Molecular modeling study revealed that BPA bound into BHb central cavity, and the binding mode of BPA-BHb complex could be hydrogen bonding. The UV-Vis absorption and CD spectra indicated that the secondary structure of BHb was altered, which may affect physiological functions of hemoglobin. This work is helpful for clarifying the molecular toxic mechanism of BPA in vivo.
采用荧光光谱法、紫外-可见吸收光谱法、圆二色谱法和分子模拟法研究了双酚 A（BPA）在生理条件下与牛血红蛋白（BHb）的相互作用。实验结果表明，BPA 可以与 BHb 结合形成复合物。计算得到结合常数 Ka 和结合位点数 n 分别为 1.49×10(5) L·mol(-1)和 1。分子模拟研究表明，BPA 结合到 BHb 的中心腔中，BPA-BHb 复合物的结合方式可能是氢键。紫外-可见吸收光谱和圆二色谱表明 BHb 的二级结构发生了变化，这可能会影响血红蛋白的生理功能。该工作有助于阐明 BPA 在体内的分子毒性机制。
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