头孢噻肟钠和氯霉素与牛血清白蛋白相互作用的荧光光谱分析

刘保生; 王晶; 薛春丽; 杨超; 吕运开

doi:10.3788/fgxb20113206.0628

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头孢噻肟钠和氯霉素与牛血清白蛋白相互作用的荧光光谱分析

光谱分析 | 更新时间：2020-08-12

- 头孢噻肟钠和氯霉素与牛血清白蛋白相互作用的荧光光谱分析
- Fluorescence Analysis of The Interaction Between Cefotaxime Sodium and Chloramphenicol as Well as Bovine Serum Albumin
- 发光学报 2011年32卷第6期页码：628-635
- 作者机构：
  
  河北大学化学与环境科学学院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：
  
  国家自然科学基金(20675024)();河北省重点基础研究项目(10967126D)资助项目。()
- DOI：10.3788/fgxb20113206.0628
  中图分类号： O657.3
- 收稿日期：2010-09-13，
  
  修回日期：2010-12-08，
  
  网络出版日期：2011-06-22，
  
  纸质出版日期：2011-06-22
- 稿件说明：
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刘保生, 王晶, 薛春丽, 杨超, 吕运开. 头孢噻肟钠和氯霉素与牛血清白蛋白相互作用的荧光光谱分析[J]. 发光学报, 2011,32(6): 628-635

LIU Bao-sheng, WANG Jing, XUE Chun-li, YANG Chao, LV Yun-kai. Fluorescence Analysis of The Interaction Between Cefotaxime Sodium and Chloramphenicol as Well as Bovine Serum Albumin[J]. Chinese Journal of Luminescence, 2011,32(6): 628-635
刘保生, 王晶, 薛春丽, 杨超, 吕运开. 头孢噻肟钠和氯霉素与牛血清白蛋白相互作用的荧光光谱分析[J]. 发光学报, 2011,32(6): 628-635 DOI： 10.3788/fgxb20113206.0628.

LIU Bao-sheng, WANG Jing, XUE Chun-li, YANG Chao, LV Yun-kai. Fluorescence Analysis of The Interaction Between Cefotaxime Sodium and Chloramphenicol as Well as Bovine Serum Albumin[J]. Chinese Journal of Luminescence, 2011,32(6): 628-635 DOI： 10.3788/fgxb20113206.0628.

摘要

在pH=7.40 Tris-HCl缓冲溶液中

应用荧光光谱法分别研究了298

303

308 K时

头孢噻肟钠(CTX)、氯霉素(CHL)对牛血清白蛋白(BSA)荧光的猝灭反应。结果表明:药物与BSA的结合稳定常数

a随温度增加而降低

两种药物对BSA的荧光猝灭皆为静态猝灭过程。标记竞争实验表明CTX、CHL在BSA中的结合位置主要位于亚域ⅡA的位点Ⅰ。在BSA-CTX(BSA-CHL)体系中再加入CHL(CTX)时

可使BSA的荧光进一步猝灭

a减小

三元体系的Hill系数均小于1

表明一种药物的存在将影响另一种药物与BSA的结合

两种药物之间具有负协同作用。用热力学参数确定了药物与BSA的作用力类型。

Abstract

In Tris-HCl buffer medium of pH 7.40

the binding reaction between cefotaxime sodium (CTX) and chloramphenicol (CHL) with bovine serum albumin (BSA) at different temperatures was studied by fluorescence spectroscopy. The results show that the values of binding constants decrease with the increasing temperature

the quenching mechanism of the combination for BSA and drugs is a static procedure. In addition

the competitive experiments suggest that the primary binding site for both CTX and CHL are located at site Ⅰ in sub-domain ⅡA of BSA. The values of Hill's coefficients are approximately equal to 1 in the binary systems

which indicate no cooperativeness in the drug's binding with BSA. The fluorescence would quench to a larger degree when CTX (or CHL) is added to the system of BSA-CHL (or BSA-CTX). Binding constants of one drug with BSA decrease when the other drug is added. Hill's coefficients of the ternary systems are less than 1. It showed that the negative cooperativity is found when CTX and CHL bound to BSA simultaneously. Thermodynamic parameters indicate that the electrostatic interaction playes a major role in the binding of drugs with BSA.

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references

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