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光谱法研究高良姜素与人血清白蛋白的相互作用

薛燕斌 乔华 李波 丁伟 孙体健

食品工业科技2017,Vol.38Issue(18):65-68,73,5.
食品工业科技2017,Vol.38Issue(18):65-68,73,5.DOI:10.13386/j.issn1002-0306.2017.18.013

光谱法研究高良姜素与人血清白蛋白的相互作用

Spectroscopic analysis of interaction between galangin and human serum albumin

薛燕斌 1乔华 2李波 1丁伟 1孙体健1

作者信息

  • 1. 山西医科大学基础医学院,山西太原030001
  • 2. 山西医科大学药学院,山西太原030001
  • 折叠

摘要

Abstract

Under the imitated physiological condition,the interaction between galangin and human serum albumin (HSA)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 HSA fluorescence in a static mode,during which hydrogen bond and Van Edward force played dominant roles.The binding constants (Ka) and site numbers (n) obtained at different temperatures were 1.26 × 106 L/mol,l.17(290.15 K),4.34 × 105 L/mol,1.09(296.15 K),1.23 × 105 L/mol,1.00(303.15 K),9.87 × 104 L/mol,0.99 (310.15 K),respectively.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 HAS were slighter.

关键词

高良姜素/人血清白蛋白/相互作用/同步荧光光谱/三维荧光光谱/圆二色谱

Key words

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

分类

轻工纺织

引用本文复制引用

薛燕斌,乔华,李波,丁伟,孙体健..光谱法研究高良姜素与人血清白蛋白的相互作用[J].食品工业科技,2017,38(18):65-68,73,5.

基金项目

山西省自然科学基金(2015011024). (2015011024)

食品工业科技

OA北大核心CSCDCSTPCD

1002-0306

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