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高良姜素与牛血清白蛋白作用的光谱研究

乔华 薛燕斌 葛琳 孙体健

天然产物研究与开发2017,Vol.29Issue(6):903-908,6.
天然产物研究与开发2017,Vol.29Issue(6):903-908,6.DOI:10.16333/j.1001-6880.2017.6.001

高良姜素与牛血清白蛋白作用的光谱研究

Spectroscopic Analysis of Interaction between Galangin and Bovine Serum Albumin

乔华 1薛燕斌 2葛琳 3孙体健1

作者信息

  • 1. 山西医科大学基础医学院
  • 2. 山西医科大学药学院
  • 3. 中国科学院山西煤炭化学研究所 分析测试中心,太原030001
  • 折叠

摘要

Abstract

The interaction between galangin and bovine serum albumin (BSA) was studied by fluorescence quenching,synchronous fluorescence,three-dimensional fluorescence and circular dichroism spectra.The results suggested that galangin had a strong ability to quench the BSA fluorescence in a static mode.The binding constants (Ka) and site numbers (n) obtained at different temperatures were 9.33 × 106 L/mol,1.17 (290.15 K);2.34 × 106 L/mol,1.09 (296.15 K);4.57 × 105 L/mol,1.01 (303.15 K);1.02 × 105 L/mol,0.99 (310.15 K),respectively.According to the thermodynamic parameters,hydrogen bond and van Edward force played dominant roles in the interaction between galangin and BSA.While the competitive binding analysis showed that the binding location of galangin to BSA is the Site I of the hydrophobic pocket.Spectra of synchronous fluorescence,three-dimensional fluorescence and circular dichroism revealed that galangin interacted with tryptophan residues in BSA more strongly than with tyrosine residues,and the vicinity of tryptophan residues was less hydrophobic.However,conformational changes of α-helix were slighter.

关键词

高良姜素/牛血清白蛋白/同步荧光光谱/三维荧光光谱/圆二色谱

Key words

galangin/bovine serum albumin/synchronous fluorescence spectra/three-dimensional fluorescence spectra/circular dichroism spectra

分类

轻工纺织

引用本文复制引用

乔华,薛燕斌,葛琳,孙体健..高良姜素与牛血清白蛋白作用的光谱研究[J].天然产物研究与开发,2017,29(6):903-908,6.

基金项目

山西省自然科学基金(2015011024) (2015011024)

天然产物研究与开发

OA北大核心CSCDCSTPCD

1001-6880

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