SIOC English
化学学报
高级检索

化学学报 ›› 2006, Vol. 64 ›› Issue (13): 1361-1366. 上一篇    下一篇

研究论文

5,7-二羟基-4'-甲氧基二氢黄酮与牛血清白蛋白的相互作用研究

王勇1，李林玺1，赵东保1,2，张卫1，刘绣华*,1,2   

  1. (1河南大学化学化工学院 开封 475001)
    (2河南大学天然产物与药物化学研究所 开封 475001)
  • 投稿日期:2005-09-13 修回日期:2006-03-14 发布日期:2006-07-14
  • 通讯作者: 刘绣华

Studies on the Interaction between 5,7-Dihydroxy-4'-methoxyflavanone and Bovine Serum Albumin

WANG Yong1, LI Lin-Xi1, ZHAO Dong-Bao1,2, ZHANG Wei1, LIU Xiu-Hua*,1,2   

  1. (1 College of Chemistry and Chemical Engineering, Henan University, Kaifeng 475001)
    (2 Institute of Natural Products and Medicine Chemistry, Henan University, Kaifeng 475001)
  • Received:2005-09-13 Revised:2006-03-14 Published:2006-07-14
  • Contact: LIU Xiu-Hua

PDF

904

被引次数

76

应用荧光光谱、紫外吸收光谱和核磁共振波谱研究了5,7-二羟基-4'-甲氧基二氢黄酮(ISO)与牛血清白蛋白(BSA)分子间的相互作用. 研究表明: ISO对BSA内源性荧光的猝灭机制属于ISO和BSA形成化合物所引起的静态猝灭; 二者的结合常数为7.41×1011 L/mol, 结合位点数为1.98. ISO与BSA作用的活性部位为其分子内的7-OH和5-OH, 且7-OH活性强于5-OH, 并且随着ISO浓度增大, BSA的构象发生了变化.

关键词: 5,7-二羟基-4'-甲氧基二氢黄酮, 牛血清白蛋白, 相互作用

The interaction between 5,7-dihydroxy-4'-methoxyflavanone (isosakuranetin, ISO) and bovine serum albumin isosakuranetin (BSA) has been investigated by fluorescence, UV absorption spectra and NMR spectroscopy. The results show that the mechanism of quenching the inner fluorescence of BSA is due to the combination of BSA with ISO which results in static quenching procedure. The binding constant is 7.41×1011 L/mol and the number of binding sites is 1.98. The active groups of ISO interacting with BSA are 7-OH and 5-OH, and 7-OH is more active than 5-OH. With the increase of ISO concentration, the conformation of BSA has been changed.

Key words: 5,7-dihydroxy-4'-methoxyflavanone, bovine serum albumin, interaction