化学学报 ›› 2010, Vol. 68 ›› Issue (01): 55-61. 上一篇    下一篇

研究论文

中药小分子阿魏酸和丹皮酚与人血清白蛋白的竞争结合作用研究

雷根虎1,刘丽亭1,戴小军1,2,卫引茂*,1,龚波林*,2   

  1. (1西北大学合成与天然功能分子化学教育部重点实验室 化学与材料科学学院 西安 710069)
    (2宁夏大学能源化工重点实验室 银川 750021)
  • 收稿日期:2009-04-10 修回日期:2009-07-26 出版日期:2010-01-14 发布日期:2010-01-20
  • 通讯作者: 卫引茂 E-mail:ymwei@nwu.edu.cn

Investigation on the Competition Interaction of Ferulic Acid and Paeonol with Human Serum Albumin by High-performance Affinity Chromatography

Lei Genhu1 Liu Liting1 Dai Xiaojun1,2 Wei Yinmao*,1 Gong Bolin*,2   

  1. (1 Key Laboratory of Synthetic and Natural Function Molecule Chemistry of Ministry of Education, College of Chemistry & Material Science, Northwest University, Xi'an 710069)
    (2 Key Laboratory of Energy & Chemical Engineering, Ningxia University, Yinchuan 750021)
  • Received:2009-04-10 Revised:2009-07-26 Online:2010-01-14 Published:2010-01-20

用亲和色谱研究了两种中药小分子阿魏酸(FA)、丹皮酚(PAE)在人体生理条件缓冲溶液(pH 7.4)条件下与人血清白蛋白(HSA)的相互作用. 从药物分子在蛋白质分子上有多种类型相互独立的结合位点的假定出发, 应用Langmuir吸附模型和竞争置换分析研究了FA, PAE与HSA的竞争性相互作用. 结果表明, FA, PAE与HSA之间存在一类位点, 且FA与PAE竞争HSA上的indole位点(site II). 根据热力学参数推测出FA, PAE与HSA之间的作用力主要为氢键作用. 从FA, PAE竞争HSA上同一位点的角度, 对中医用药中常将含有FA与含有PAE的中药配伍使用, 以提高疗效的临床用药现象进行了解释.

关键词: 亲和色谱, 人血清白蛋白, 阿魏酸, 丹皮酚, 小分子-生物大分子相互作用

The competition interaction of two active components of Chinese traditional herb, ferulic acid (FA) and paeonol (PAE), with immobilized human serum albumin (HSA) on chromatographic support under human physiological condition (pH 7.4) has been investigated by high-performance affinity chromatography (HPAC). Based upon the assumption that there were several independent types of binding sites on an HSA molecule for each drug, the interaction of immobilized HSA with FA and PAE was investigated by frontal analysis and competition displacement analysis. The results showed that there was only a single binding site in the HSA molecule for FA and PAE. As FA and PAE coexisted, they had a direct competition for the indole site (site II) of HSA molecule. According to the thermodynamic parameters, the main force between HSA and FA or PAE was deduced to be hydrogen bonding. The conclusion that both PAE and FA competed with each other for the same binding site of HSA molecule could be used to explain some phenomena in the Chinese medicine clinic, in which the clinical efficacy of each drug can be improved by utilizing the compatibility of Chinese traditional medicine.

Key words: high-performance affinity chromatography, human serum album, ferulic acid, paeonol, small molecular-biopolymer interaction