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Interaction of Emodin and its Derivative Frangulin-A with Bovine Serum Albumin and Calf Thymus DNA
Journal of Applied Spectroscopy ( IF 0.8 ) Pub Date : 2020-03-26 , DOI: 10.1007/s10812-020-00961-z
X.-X. Hu , Zh.-F. Huang , G.-Sh. Lu , J.-Y. Huang , X. Tan , G.-T. Huang

The interaction between emodin, frangulin-A (obtained from Ventilago leiocarpa Benth) with bovine serum albumin (BSA), and calf thymus DNA (ct-DNA) has been investigated. The fluorescence spectrum and molecular docking methods are used to investigate the interaction between emodin, frangulin-A, and BSA. The UV spectrum revealed interaction between emodin, frangulin-A, and ct-DNA. The fluorescence spectrum confirmed that the compounds of emodin–BSA and frangulin-A–BSA were formed showing fl uorescence quenching and a decrease of the maximum emission wavelength. The simulated molecular docking showed stable combinations of emodin–BSA and frangulin-A– BSA. Thus, molecular interactions mainly occur due to hydrophobic forces and hydrogen bonds. According to the UV spectrum, emodin and frangulin-A interacted with ct-DNA via electrostatic interaction.

中文翻译:

大黄素及其衍生物Frangulin-A与牛血清白蛋白和小牛胸腺DNA的相互作用

已经研究了大黄素,乳清蛋白-A(从Leocarpa Benth获得)与牛血清白蛋白(BSA)和小牛胸腺DNA(ct-DNA)之间的相互作用。荧光光谱和分子对接方法用于研究大黄素,乳腺素A和BSA之间的相互作用。紫外光谱揭示了大黄素,促性腺素A和ct-DNA之间的相互作用。荧光光谱证实形成了大黄素-BSA和霜蛋白-A-BSA化合物,显示出荧光猝灭和最大发射波长的减小。模拟的分子对接显示大黄素-BSA和乳蛋白-A-BSA的稳定组合。因此,分子相互作用主要由于疏水力和氢键而发生。根据紫外光谱,大黄素和乳蛋白-A通过静电相互作用与ct-DNA相互作用。
更新日期:2020-03-26
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