高等学校化学学报 ›› 1994, Vol. 15 ›› Issue (3): 373.

• 论文 • 上一篇    下一篇

蒽醌及黄酮类化合物与人血清白蛋白的结合反应研究

张保林1, 王文清2, 白凤莲3   

  1. 1. 南京大学配位化学研究所, 配位化学国家重点实验室, 南京, 210008;
    2. 北京大学技术物理系;
    3. 中国科学院化学研究所, 北京
  • 收稿日期:1993-03-01 修回日期:1993-08-17 出版日期:1994-03-24 发布日期:1994-03-24
  • 通讯作者: 张保林,男,28岁,博士,博士后.
  • 作者简介:张保林,男,28岁,博士,博士后.
  • 基金资助:

    国家自然科学基金

Studies on the Binding of Anthraquinones and Flavonoids to Human Serum Albumin

ZHANG Bao-Lin1, WANG Wen-Qing2, BAI Feng-Lian3   

  1. 1. Coordination Chemistry Institute of Nanjing University, State Key Laboratory of Coordination Chemistry, Nanjing, 210008;
    2. Technical Physics Department of Peking University;
    3. Institute of Chemistry, Chinese Academy of Sciences
  • Received:1993-03-01 Revised:1993-08-17 Online:1994-03-24 Published:1994-03-24

摘要: 用荧光光谱法研究了大黄素、黄酮、栎精、柚皮甙、黄芩甙和龙胆苦甙等化合物与人血清白蛋白(HSA)的结合反应。发现除龙胆苦甙外,其余化合物对HSA的荧光有很强的猝灭作用。从荧光猝灭结果求得了它们与HSA的结合常数,表明这些化合物与HSA的结合能力随其所含极性基团的增多而减弱。根据Forster非辐射能量转移机理,求出了第一结合部位与HSA分子中214-色氨酸残基的距离,由此提出了形成复合物的结构模型。并对油酸钠与大黄素、黄酮的竞争结合反应和黄芩甙与大黄素、栎精之间的竞争结合反应进行了研究。

关键词: 蒽醌和黄酮类化合物, 人血清白蛋白, 结合, 荧光光谱

Abstract: The binding of emodin, flavone,quercetin, naringin, baicalin and gentiopicrin to human serum albumin (HSA) was studied using fluorescence spectroscopy.It was shown that these compounds have a powerful ability to quench the HSAfluorescence via a nonradiative energy transfer mechanism except gentiopicrin.The fluorescence quenching data was analyzed according to Scatchard equation,and the binding constants in the range 104 to 5×105L/mol were obtained.It was found that the affinity of these compounds to HSAis positively related to their hydrophobicity.By use of a spectra overlap integral between the absorption spectrum of these compounds and the emission spectrum for HSA, the distance of Trp-214residue to the first binding site of these compounds was estimated.In addition, the competition binding of oleate with emodin and flavone, baicalin with emodin and quercetin was monitored by fluorescence quenching.The binding mechanism was discussed in brief and an allosteric domain model of emodin-HSAcomplex was postulated from above results.

Key words: Anthraquinones and flavonoids, Human serum albumin, Binding, Fluorescence spectrum

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