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黄芩与牛血清白蛋白相互作用的光谱特性研究

李晨男 柳晓婷 王乐新

黑龙江八一农垦大学学报2026,Vol.38Issue(2):63-68,92,7.
黑龙江八一农垦大学学报2026,Vol.38Issue(2):63-68,92,7.DOI:10.3969/j.issn.1002-2090.2026.02.009

黄芩与牛血清白蛋白相互作用的光谱特性研究

Spectral Characteristics of the Interaction between Scutellaria Baicalensis Georgi and Bovine Serum Albumin

李晨男 1柳晓婷 2王乐新3

作者信息

  • 1. 黑龙江八一农垦大学食品学院,大庆 163319
  • 2. 黑龙江八一农垦大学信息与电气工程学院
  • 3. 黑龙江八一农垦大学理学院
  • 折叠

摘要

Abstract

To investigate the interaction mechanism of scutellaria baicalensis georgi(SBG)produced in Daqing with bovine serum albumin(BSA),the aqueous extract of SBG was used as the material.The interaction mechanism,main binding forces,thermodynamic parameters,and binding sites were determined by fluorescence spectroscopy.The results showed that the fluorescence intensity of BSA was regularly quenched with the increase of SBG aqueous extract concentration,and the fluorescence peak exhibited a red shift of 6 nm,indicating the occurrence of binding and enhanced polarity of the microenvironment around tryptophan residues.Based on the binding number less than one and the thermodynamic parameters(△H>0,and △S>0,△G<0),it was concluded that SBG showed weak binding ability to BSA,and the interaction was driven mainly by hydrophobic forces.Synchronous fluorescence spectroscopy further revealed that the polarity of the tryptophan microenvironment was increased and hydrophobicity was decreased,while the conformation tyrosine residues was not significantly changed,suggesting that the interaction primarily occurred near tryptophan residues.This study helps clarify the binding mechanism of SBG with BSA and provides theoretical and experimental data for understanding the behavior of SBG in blood circulation.

关键词

黄芩/牛血清白蛋白/荧光光谱/荧光猝灭

Key words

Scutellaria baicalensis georgi/bovine serum albumin/fluorescence spectroscopy/fluorescence quenching

分类

生物科学

引用本文复制引用

李晨男,柳晓婷,王乐新..黄芩与牛血清白蛋白相互作用的光谱特性研究[J].黑龙江八一农垦大学学报,2026,38(2):63-68,92,7.

基金项目

黑龙江省自然基金资助项目(F201427). (F201427)

黑龙江八一农垦大学学报

1002-2090

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