Here we synthesized four 3-fluorooxindole derivatives and investigated their affinity interactions with serum albumin by using multi-spectral, electrochemical, and molecular docking. Fluorescence spectroscopy results revealed the affinity of 3-fluorooxindole derivatives and serum albumin. UV spectroscopy showed the type of quenching for both were static quenching, which was proved by temperature dependence experiments and time-resolved fluorescence. Electrochemical experiment results suggested the binding constant of 3-fluorooxindole derivatives and serum albumin was 10³–10⁴ by the order of magnitude. Synchronous fluorescence spectroscopy and infrared spectroscopy demonstrated the effect on the secondary structure of serum albumin in the presence of 3-fluorooxindole units. Furthermore, molecular docking and site competition experiments result determined that 3-fluorooxindole derivatives bind to site I of serum albumin. Finally, the interactions between 3-fluorooxindole derivatives and serum albumin were investigated by various methods and summarized the effects of substituents in 3-fluorooxindole derivatives on serum albumin interactions. These results provide a reference for the design of subsequent synthesis of 3-fluorooxindole derivatives and theoretical support for the development of related fluorine-containing drugs.

在这里，我们合成了四种 3-氟羟吲哚衍生物，并通过使用多光谱、电化学和分子对接研究了它们与血清白蛋白的亲和相互作用。荧光光谱结果揭示了 3-氟羟吲哚衍生物和血清白蛋白的亲和力。紫外光谱表明两者的猝灭类型都是静态猝灭，这通过温度依赖性实验和时间分辨荧光得到证实。电化学实验结果表明3-氟羟吲哚衍生物与血清白蛋白的结合常数为10 ³ –10 ⁴按数量级。同步荧光光谱和红外光谱证明了在 3-氟吲哚单元存在下对血清白蛋白二级结构的影响。此外，分子对接和位点竞争实验结果确定 3-氟羟吲哚衍生物与血清白蛋白的位点 I 结合。最后，通过各种方法研究了 3-氟羟吲哚衍生物与血清白蛋白之间的相互作用，并总结了 3-氟羟吲哚衍生物中取代基对血清白蛋白相互作用的影响。这些结果为后续合成3-氟羟吲哚衍生物的设计提供了参考，并为相关含氟药物的开发提供了理论支持。