两种肉桂酸肟酯衍生物的合成及其与人血清白蛋白的结合
发布时间：2019-04-19 05:39
【摘要】：以间甲氧基肉桂酸、对位取代的苯甲醛为原料,设计合成了2种未见报道的肉桂酸肟酯类衍生物,并用MS、IR、1H NMR、13C NMR进行结构表征。采用分子对接技术和荧光光谱法、紫外-可见光谱法、位点竞争法研究了2种衍生物分别和人血清白蛋白(HSA)相结合的机理。通过Stern-Volmer方程等处理荧光猝灭相关数据得到了衍生物与HSA相互作用的结合常数和热力学参数。结合紫外-可见光谱对两种衍生物与HSA的相互作用进行了进一步的分析,结果表明在体外生理条件下,衍生物都可以与HSA结合,对HSA内源荧光产生静态猝灭并对其构象产生影响,其主要的结合力为氢键和范德华力。位点竞争实验表明衍生物与HSA相互作用都发生在Sudlow site 1(亚域ⅡA)处。以上实验结果均验证了分子模拟对实验的预测。
[Abstract]:Using m-methoxycinnamic acid and p-substituted benzaldehyde as raw materials, two derivatives of oxime cinnamate esters were designed and synthesized, and their structures were characterized by MS,IR,1H NMR,13C NMR. The binding mechanism of the two derivatives to human serum albumin (HSA) was studied by molecular docking technique, fluorescence spectroscopy, UV-vis spectroscopy and site competition method. The binding constants and thermodynamic parameters of the interaction between the derivatives and HSA were obtained by processing the fluorescence quenching data by Stern-Volmer equation. The interaction between the two derivatives and HSA was further analyzed by UV-vis spectroscopy. The results showed that both derivatives could bind to HSA under physiological conditions in vitro. The static quenching and conformation of HSA were induced by endogenous fluorescence. The main binding forces were hydrogen bond and van der Waals force. Site competition test showed that the interaction between derivatives and HSA occurred at the site of Sudlow site-1 (subdomain 鈪，
本文编号：2460649
[Abstract]:Using m-methoxycinnamic acid and p-substituted benzaldehyde as raw materials, two derivatives of oxime cinnamate esters were designed and synthesized, and their structures were characterized by MS,IR,1H NMR,13C NMR. The binding mechanism of the two derivatives to human serum albumin (HSA) was studied by molecular docking technique, fluorescence spectroscopy, UV-vis spectroscopy and site competition method. The binding constants and thermodynamic parameters of the interaction between the derivatives and HSA were obtained by processing the fluorescence quenching data by Stern-Volmer equation. The interaction between the two derivatives and HSA was further analyzed by UV-vis spectroscopy. The results showed that both derivatives could bind to HSA under physiological conditions in vitro. The static quenching and conformation of HSA were induced by endogenous fluorescence. The main binding forces were hydrogen bond and van der Waals force. Site competition test showed that the interaction between derivatives and HSA occurred at the site of Sudlow site-1 (subdomain 鈪，
本文编号：2460649
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