吡格列酮与白蛋白相互作用的荧光光谱和分子对接研究。
Interaction study of pioglitazone with albumin by fluorescence spectroscopy and molecular docking.
机构信息
Endocrinology and Metabolism Research Center, Tehran University of Medical Sciences, Tehran, Iran.
出版信息
Spectrochim Acta A Mol Biomol Spectrosc. 2011 Jan;78(1):96-101. doi: 10.1016/j.saa.2010.09.001. Epub 2010 Sep 17.
Pioglitazone is a medicine of thiazolidinedione (TZD) class with hypoglycemic (antihyperglycemic, antidiabetic) action. Pioglitazone binding to human serum albumin (HSA) was investigated at different temperatures (290, 300 and 310 K) by fluorescence spectroscopic method. Molecular docking study was also carried out besides the experiments. Experimental results revealed that pioglitazone have an ability to quench the intrinsic fluorescence of HSA tryptophan through a static quenching procedure. The binding constant was determined using Stern-Volmer modified equation and energy transfer mechanisms of quenching were discussed. Thermodynamic parameters were also calculated according to enthalpy changes dependence on different temperatures. According to the theoretical and experimental results, hydrogen bonding was found to play a major role in the interaction of pioglitazone with HSA.
吡格列酮是噻唑烷二酮（TZD）类具有降血糖（抗高血糖、抗糖尿病）作用的药物。荧光光谱法研究了吡格列酮在不同温度（290、300 和 310 K）下与人血清白蛋白（HSA）的结合情况。除了实验之外，还进行了分子对接研究。实验结果表明，吡格列酮通过静态猝灭过程具有猝灭 HSA 色氨酸内源荧光的能力。使用 Stern-Volmer 修正方程确定结合常数，并讨论猝灭的能量转移机制。还根据焓随不同温度的变化计算了热力学参数。根据理论和实验结果，发现氢键在吡格列酮与 HSA 的相互作用中起主要作用。
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