Luminescence Mechanism Study of The Conjugation Reaction between Cefpirome Sulfate and Bovine Serum Albumin

LIU Bao-sheng; YANG Chao; WANG Jing; XUE Chun-li; LU Yun-kai

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Luminescence Mechanism Study of The Conjugation Reaction between Cefpirome Sulfate and Bovine Serum Albumin

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- Luminescence Mechanism Study of The Conjugation Reaction between Cefpirome Sulfate and Bovine Serum Albumin
- Chinese Journal of Luminescence Vol. 32, Issue 3, Pages: 293-299(2011)
- 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：
  CLC： O657.3;O482.31
- Received：29 October 2010，
  
  Revised：15 November 2010，
  
  Published Online：22 March 2011，
  
  Published：22 March 2011
- 稿件说明：
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刘保生, 杨超, 王晶, 薛春丽, 吕运开. 硫酸头孢匹罗与牛血清白蛋白结合反应的发光机理[J]. 发光学报, 2011,32(3): 293-299

LIU Bao-sheng, YANG Chao, WANG Jing, XUE Chun-li, LU Yun-kai. Luminescence Mechanism Study of The Conjugation Reaction between Cefpirome Sulfate and Bovine Serum Albumin[J]. Chinese Journal of Luminescence, 2011,32(3): 293-299
刘保生, 杨超, 王晶, 薛春丽, 吕运开. 硫酸头孢匹罗与牛血清白蛋白结合反应的发光机理[J]. 发光学报, 2011,32(3): 293-299 DOI：

LIU Bao-sheng, YANG Chao, WANG Jing, XUE Chun-li, LU Yun-kai. Luminescence Mechanism Study of The Conjugation Reaction between Cefpirome Sulfate and Bovine Serum Albumin[J]. Chinese Journal of Luminescence, 2011,32(3): 293-299 DOI：

摘要

在人生理条件下

利用荧光猝灭法、同步荧光法及共振光散射法

分别研究了不同温度下硫酸头孢匹罗(CPS)与牛血清白蛋白(BSA)间的结合反应。结果表明:随着CPS浓度的增加

BSA的荧光、共振散射光依次降低

其荧光猝灭为静态猝灭过程并伴随非辐射能量转移作用。反应的结合常数为10

数量级

结合位点数约为1;结合位点位于BSA的亚结构ⅡA中;结合距离

＜7 nm。CPS与BSA间作用力主要是静电引力;Hill系数

＜1

表明CPS有弱的负协同作用。同步荧光光谱表明CPS对BSA构象产生影响

使BSA腔内疏水环境的极性增强

疏水性减弱。

Abstract

In human physical conditions

the binding reaction between cefpirome sulfate (CPS) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy

synchronous fluorescence spectroscopy and resonance light scattering (RLS) at different temperatures. Results showed that both fluorescence and RLS of BSA reduced with the increased concentration of CPS

and the effect between CPS and BSA was static fluorescence quenching process with Frester spectroscopy energy transfer. The scope of apparent binding constants (

) was ~10

; the corresponding binding site value (

) in the binary systems was 1; the binding distances (

) were much smaller than 7 nm and the primary binding site for CPS was located at site Ⅰ in sub-domain ⅡA of BSA. Besides

the electrostatic attraction plays an important role in the conjugation reaction of BSA and CPS. The values of Hills coefficients were less than 1

which indicated that there was some negative cooperative effect. Studies utilizing synchronous spectra showed that the conjugation reaction between CPS and BSA would affect the conformation of BSA

leading to the polarity around BSA strengthened and the hydrophobicity weakened.

关键词

Keywords

references

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