In this article, the interaction between six fluoroquinolones (FQs) and bovine serum albumin (BSA) was initially studied at 298 K, 303 K and 310 K respectively under simulated physiological conditions by fluorescence spectroscopy. At the same time, the sub-structural domains on BSA that may bind to FQs were investigated by molecular docking simulation technique. A combination of quantitative and qualitative approaches was used in the analysis of the binding constants, binding sites and corresponding thermodynamic parameters in the interaction system, it was found that FQs forms a complex with BSA and undergoes static quenching, which is the main cause of fluorescence quenching. The results indicated that hydrogen bonds, Van der Waals force and electrostatic interaction were the main binding forces between the complexes, it also showed that these six fluoroquinolones mainly bound to the IIA and IIIA structural domains of BSA, while DANO and SARA may be more toxic than other antibiotics. Based on Foster's non-radiative energy transfer theory, the binding distance between FQs and BSA was calculated to be less than 7 nm, indicating the existence of energy transfer between small molecule drugs and proteins. Synchronous fluorescence and UV–Vis absorption spectroscopy further confirmed that FQs can alter the secondary conformational change of BSA. Lomefloxacin has a different effect from the other five fluoroquinolone antibiotics because it causes a decrease in polarity and an increase in hydrophobicity around tryptophan residues, while the other five FQs have the opposite effect. Together, the study of FQs-BSA is of great significance to elucidate the pharmacokinetics and pharmacodynamics of FQs.

在本文中，通过荧光光谱在模拟生理条件下分别在 298 K、303 K 和 310 K 下初步研究了六种氟喹诺酮类药物 (FQs) 与牛血清白蛋白 (BSA) 之间的相互作用。同时，通过分子对接模拟技术研究了BSA上可能与FQs结合的子结构域。采用定量和定性相结合的方法对相互作用体系中的结合常数、结合位点和相应的热力学参数进行分析，发现FQs与BSA形成复合物并发生静态猝灭，这是产生荧光的主要原因淬火。结果表明，氢键、范德华力和静电相互作用是配合物之间的主要结合力，它还表明，这六种氟喹诺酮类主要与 BSA 的 IIA 和 IIIA 结构域结合，而 DANO 和 SARA 可能比其他抗生素毒性更大。基于 Foster 的非辐射能量转移理论，计算出 FQ 与 BSA 的结合距离小于 7 nm，表明小分子药物与蛋白质之间存在能量转移。同步荧光和紫外-可见吸收光谱进一步证实 FQs 可以改变 BSA 的二级构象变化。洛美沙星与其他五种氟喹诺酮类抗生素的作用不同，因为它会导致色氨酸残基周围的极性降低和疏水性增加，而其他五种 FQ 则具有相反的作用。一起，