光谱法研究 4-氨基安替比林与牛血红蛋白的毒理相互作用。
Spectroscopic investigation on the toxicological interactions of 4-aminoantipyrine with bovine hemoglobin.
机构信息
Shandong Key Laboratory of Water Pollution Control and Resource Reuse, School of Environmental Science and Engineering, Shandong University, 27 Shanda South Road, Jinan, 250100, People's Republic of China.
出版信息
J Fluoresc. 2010 Jan;20(1):381-7. doi: 10.1007/s10895-009-0543-2. Epub 2009 Sep 29.
The effects of 4-aminoantipyrine (AAP) on bovine hemoglobin (BHb) were investigated by fluorescence spectroscopy, synchronous fluorescence spectroscopy, ultraviolet-visible absorption spectroscopy and circular dichroism spectroscopy (CD) under simulated physiological conditions. The experimental results showed that AAP effectively quenched the intrinsic fluorescence of BHb via static quenching. The number of binding sites, the binding constant K(a), and the thermodynamic parameters (DeltaH(o), DeltaS(o) and DeltaG(o)) were measured at two different temperatures. Van der Waals' interactions and hydrogen bonds were the predominant intermolecular forces in stabilizing the BHb-AAP complex. The experiment results confirmed micro-environmental and conformational changes of BHb in the presence of AAP. The alpha-helix content decreased, indicating that AAP destroys some of the hydrogen bonding networks in the polypeptide chain.
在模拟生理条件下，通过荧光光谱法、同步荧光光谱法、紫外可见吸收光谱法和圆二色光谱法（CD）研究了 4-氨基安替比林（AAP）对牛血红蛋白（BHb）的影响。实验结果表明，AAP 通过静态猝灭有效地猝灭了 BHb 的固有荧光。在两个不同温度下测量了结合位点数、结合常数 K(a)和热力学参数（ΔH(o)、ΔS(o)和ΔG(o)）。范德华相互作用和氢键是稳定 BHb-AAP 配合物的主要分子间力。实验结果证实了 AAP 存在时 BHb 的微环境和构象变化。α-螺旋含量降低，表明 AAP 破坏了多肽链中的一些氢键网络。
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