School of Chemical Biology and Pharmaceutical Sciences, Capital Medical University, Beijing 100069, PR China.
Spectrochim Acta A Mol Biomol Spectrosc. 2010 May;75(5):1506-10. doi: 10.1016/j.saa.2010.02.007. Epub 2010 Feb 11.
The interaction between hyperoside and bovine serum albumin (BSA) was examined by fluorescence spectroscopy at 298, 304, and 310K. The spectroscopic data were analyzed using Tachiya model and Stern-Volmer equation to determine the binding sites and apparent binding constant between hyperoside and BSA. For Tachiya model, both binding sites and apparent binding constants increased with the increasing of temperature, whereas for Stern-Volmer equation, the corresponding binding constants decreased as temperature increasing and the binding sites were independent of temperature. The positive sign of enthalpy change (DeltaH) and entropy change (DeltaS) suggested that hydrophobic forces played a major role in the interaction. Synchronous fluorescence spectra indicated that the conformation of protein was perturbed by the interaction of hyperoside with BSA. Moreover, the presence of metal ion affected the hyperoside-BSA binding.
运用荧光光谱法在 298、304 和 310K 温度下考察了桃叶珊瑚苷与牛血清白蛋白（BSA）的相互作用。利用 Tachiya 模型和 Stern-Volmer 方程对光谱数据进行分析，以确定桃叶珊瑚苷与 BSA 之间的结合部位和表观结合常数。对于 Tachiya 模型，结合部位和表观结合常数均随温度升高而增加，而对于 Stern-Volmer 方程，相应的结合常数随温度升高而降低，而结合部位则与温度无关。焓变（DeltaH）和熵变（DeltaS）为正值表明，疏水作用力在相互作用中起主要作用。同步荧光光谱表明，蛋白质的构象因桃叶珊瑚苷与 BSA 的相互作用而受到干扰。此外，金属离子的存在影响了桃叶珊瑚苷与 BSA 的结合。
