环丙沙星、氧氟沙星同时 与牛血清白蛋白分子作用的荧光光谱

刘保生; 薛春丽; 王 晶; 杨 超; 吕运开

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环丙沙星、氧氟沙星同时与牛血清白蛋白分子作用的荧光光谱

论文 | 更新时间：2020-08-12

- 环丙沙星、氧氟沙星同时与牛血清白蛋白分子作用的荧光光谱
- Studies on the Interaction between Ciprofloxacin and Ofloxacin in Presence of Bovine Serum Albumin by Spectroscopic Methods
- 发光学报 2010年31卷第2期页码：285-290
- 作者机构：
  
  河北大学理化分析中心药物化学与分子诊断教育部重点实验室,河北保定,071002
- 作者简介：
- 基金信息：
- DOI：
  中图分类号： O657.3;O482.31
- 收稿日期：2009-11-25，
  
  修回日期：1900-01-02，
  
  网络出版日期：2010-04-30，
  
  纸质出版日期：2010-04-30
- 稿件说明：
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刘保生, 薛春丽, 王晶, 等. 环丙沙星、氧氟沙星同时与牛血清白蛋白分子作用的荧光光谱[J]. 发光学报, 2010,31(2):285-290.

LIU Bao-sheng, XUE Chun-li, WANG Jing, et al. Studies on the Interaction between Ciprofloxacin and Ofloxacin in Presence of Bovine Serum Albumin by Spectroscopic Methods[J]. Chinese journal of luminescence, 2010, 31(2): 285-290.
刘保生, 薛春丽, 王晶, 等. 环丙沙星、氧氟沙星同时与牛血清白蛋白分子作用的荧光光谱[J]. 发光学报, 2010,31(2):285-290. DOI：

LIU Bao-sheng, XUE Chun-li, WANG Jing, et al. Studies on the Interaction between Ciprofloxacin and Ofloxacin in Presence of Bovine Serum Albumin by Spectroscopic Methods[J]. Chinese journal of luminescence, 2010, 31(2): 285-290. DOI：

摘要

在pH=7.40的水溶液中

环丙沙星(CPFX)、氧氟沙星(OFLX)能够猝灭牛血清白蛋白(BSA)的荧光。当两种药物共存时BSA荧光被进一步猝灭。据此建立了利用荧光发光光谱法进行喹诺酮类药物CPFX与OFLX间相互作用的研究。结果表明:药物间存在相互作用

使药物与蛋白间的结合常数减小、结合稳定性下降

游离型药物含量增加

造成药效增强;药物对蛋白荧光的猝灭属于静态猝灭

药物与蛋白结合位点数约为1。根据Frster非辐射能量转移理论

确定了药物与蛋白之间的结合距离

＜7 nm

属于非辐射能量转移。药物间的相互作

用使r

值增加

结合距离增大。同步荧光光谱研究表明药物间的相互作用对蛋白构象产生影响

使蛋白质分子伸展

疏水性降低。

Abstract

In the aqueous solution of pH=7.40

both ciprofloxacin (CPFX) and ofloxacin (OFLX) can quench fluorescence of bovine serum albumin (BSA). The fluorescence intensity is obviously gone down when the two drugs coexist. According to this

studies were established on the interaction between CPFX and OFLX by fluorescence spectrum. It was proved that the interaction between the drugs reduces the binding stability of the drug and protein. At the same time

increase of the free drug concentration will increase the effect of the drugs. The result showed that the quenching mechanism of the combination of bovine serum albumin and drugs is a static procedure. The number of binding sites is 1 in several of system. Based on the theory of Frester spectroscopy energy transfer

the binding distance (

＜7.0 nm) between the drugs and BSA was obtained. It belongs to non-radiation energy transfer. Because of the existence of interaction between the drugs

the correlation coefficient and binding distance are increased. Studies by synchronous spectra show the effect of the interaction between the drugs on conformation of BSA. It makes protein molecules extend and hydrophobic nature reduces.

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references

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