Interaction of Cefpiramide Sodium with Bovine Serum Albumin and The Effect of Coexistent Metal Ion on The Reaction

LIU Bao-sheng; YAN Xiao-na; CAO Shi-na; CHONG Bao-hong; LV Yun-kai

doi:10.3788/fgxb20123309.1018

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Interaction of Cefpiramide Sodium with Bovine Serum Albumin and The Effect of Coexistent Metal Ion on The Reaction

更新时间：2020-08-12

- Interaction of Cefpiramide Sodium with Bovine Serum Albumin and The Effect of Coexistent Metal Ion on The Reaction
- Chinese Journal of Luminescence Vol. 33, Issue 9, Pages: 1018-1024(2012)
- 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：
- DOI：10.3788/fgxb20123309.1018
  CLC： O657.3
- Received：26 March 2012，
  
  Revised：28 June 2012，
  
  Published：10 September 2012
- 稿件说明：
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刘保生, 闫潇娜, 曹世娜, 种宝红, 吕运开. 头孢匹胺钠与牛血清白蛋白的相互作用机理及共存金属离子的影响[J]. 发光学报, 2012,33(9): 1018-1024

LIU Bao-sheng, YAN Xiao-na, CAO Shi-na, CHONG Bao-hong, LV Yun-kai. Interaction of Cefpiramide Sodium with Bovine Serum Albumin and The Effect of Coexistent Metal Ion on The Reaction[J]. Chinese Journal of Luminescence, 2012,33(9): 1018-1024
刘保生, 闫潇娜, 曹世娜, 种宝红, 吕运开. 头孢匹胺钠与牛血清白蛋白的相互作用机理及共存金属离子的影响[J]. 发光学报, 2012,33(9): 1018-1024 DOI： 10.3788/fgxb20123309.1018.

LIU Bao-sheng, YAN Xiao-na, CAO Shi-na, CHONG Bao-hong, LV Yun-kai. Interaction of Cefpiramide Sodium with Bovine Serum Albumin and The Effect of Coexistent Metal Ion on The Reaction[J]. Chinese Journal of Luminescence, 2012,33(9): 1018-1024 DOI： 10.3788/fgxb20123309.1018.

摘要

研究了不同温度下牛血清白蛋白(BSA)与头孢匹胺钠(CPMS)的相互作用及常见金属离子(Mg

、Zn

、Cu

、Fe

、Co

、Ni

)对BSA-CPMS体系的影响。结果表明:CPMS能使BSA的荧光发生猝灭

其过程为静态猝灭并伴有非辐射能量转移;CPMS通过静电引力与BSA结合

结合常数为10

数量级

结合位点数约为1;结合主要作用于BSA的亚结构ⅡA中

结合距离

≈2.60 nm。同步荧光光谱和圆二色谱(CD)均表明CPMS使BSA构象发生了变化。

Abstract

The interaction between bovine serum albumin (BSA) and cefpiramide sodium (CPMS) was investigated at different temperatures. The effect of common metal ions (Mg

) on the BSA-CPMS system was also researched. The results show that CPMS can quench the intrinsic fluorescence of BSA significantly

and the quenching mechanism is a static quenching process which follows the Förester spectroscopy energy transfer. The electrostatic force played an important role on the conjugation reaction between BSA and CPMS. The binding constants (

) was in the order of 10

and the number of binding site (

) in the binary system was approximately equal to 1. The binding distance (

) was about 2.60 nm and the primary binding for CPMS was located at sub-domainⅡA of BSA. Synchronous spectra and Circular dichroism(CD) spectra revealed that the microenvironment and the conformation of BSA were changed during the conjugation reaction.

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Keywords

references

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河北大学化学与环境科学学院, 河北保定 071002

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Dingxi Teachers College, Dingxi 743000, China

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