Cui Feng-Ling, Qin Li-Xia, Zhang Gui-Sheng, Yao Xiao-Jun, Du Juan
School of Chemistry and Environmental Science, Key Laboratory for Environmental Pollution Control Technology of Henan Province, Henan Normal University, Xinxiang 453007, People's Republic of China.
Int J Biol Macromol. 2008 Apr 1;42(3):221-8. doi: 10.1016/j.ijbiomac.2007.10.013. Epub 2007 Oct 22.
This study was designed to examine the interaction of daunorubicin with human serum albumin (HSA) for the first time by fluorescence spectroscopy in combination with UV absorption and molecular modeling under simulative physiological conditions. The quenching mechanism was suggested to be static quenching according to the fluorescence measurement and the linearity of Scatchard plot indicated that daunorubicin bound to a single class of binding sites on HSA. The thermodynamic parameters, enthalpy change (DeltaH) and entropy change (DeltaS) were calculated to be -16.13 kJ/mol and 27.86 J/(molK), according to the Vant'Hoff equation. These data suggested that hydrophobic interaction was the predominant intermolecular forces stabilizing the complex, which was in good agreement with the results of molecular modeling study. In addition, the effects of common ions on the binding constant of daunorubicin-HSA complex were also discussed at room temperature. Moreover, the synchronous fluorescence technique was successfully employed to determine the total proteins in serum, urine and saliva samples at room temperature under the optimum conditions with a wide linear range and satisfactory results.
本研究旨在首次通过荧光光谱结合紫外吸收和分子模拟，在模拟生理条件下研究柔红霉素与人血清白蛋白（HSA）的相互作用。根据荧光测量结果，猝灭机制被认为是静态猝灭，Scatchard图的线性表明柔红霉素与HSA上的一类结合位点结合。根据范特霍夫方程，计算出热力学参数焓变（ΔH）和熵变（ΔS）分别为-16.13 kJ/mol和27.86 J/(mol·K)。这些数据表明疏水相互作用是稳定复合物的主要分子间作用力，这与分子模拟研究结果高度一致。此外，还讨论了室温下常见离子对柔红霉素-HSA复合物结合常数的影响。此外，在最佳条件下，同步荧光技术成功地用于室温下测定血清、尿液和唾液样品中的总蛋白，线性范围宽，结果令人满意。
