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化学学报
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化学学报 ›› 2010, Vol. 68 ›› Issue (15): 1494-1498. 上一篇    下一篇

研究论文

谱学与分子模拟研究甲磺酸酚妥拉明与肌红蛋白作用的分子机理

毛慧1，孔凡彬2，赵国政1，赵波*,1，沈敬山*,3   

  1. (1江苏省生物功能材料重点实验室 南京师范大学化学与环境科学学院 南京 210097)
    (2河南科技学院资源与环境学院 新乡 453003)
    (3中国科学院上海药物研究所 上海 201203)
  • 投稿日期:2009-08-25 修回日期:2010-03-12 发布日期:2010-04-21
  • 通讯作者: 赵波 E-mail:zhaobo@njnu.edu.cn

Molecular Modeling and Spectroscopic Studies on the Interaction between Phentolamine Mesylate and Myoglobin

Mao Hui1 Kong Fanbin 2 Zhao Guozheng 1 Zhao Bo*,1 Shen Jingshan*,3   

  1. (1 Jiangsu Key Laboratory of Biofunctional Materials, College of Chemistry and Environmental Science, Nanjing Normal University, Nanjing 210097)
    (2 School of Resource and Environment Science, Henan Institute of Science and Technology, Xinxiang 453003)
    (3 Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203)
  • Received:2009-08-25 Revised:2010-03-12 Published:2010-04-21
  • Contact: ZHAO Bo E-mail:zhaobo@njnu.edu.cn

PDF

989

被引次数

12

利用紫外吸收光谱、荧光光谱结合分子模拟技术研究了在模拟生理条件下甲磺酸酚妥拉明(phentolamine mesylate, PM)与肌红蛋白(myoglobin, Mb)的作用机制. 实验结果表明: 药物小分子甲磺酸酚妥拉明与蛋白相互作用时结合位点数为1, 表观结合常数KA为5.27×104 L•mol－1. 分子模拟结果表明: PM在Mb上的结合位点是site1活性口袋, 两者通过疏水作用、亲水作用、氢键作用以及静电作用结合. PM与Mb中的氨基酸残基Trp, Tyr和Phe发生疏水相互作用, 进而导致Mb的紫外吸收峰强度降低以及荧光的猝灭. 它们之间负的Δ 值表明结合反应是热力学允许的.

关键词: 甲磺酸酚妥拉明, 肌红蛋白, 相互作用, 分子模拟

The molecular interaction mechanism of phentolamine mesylate (PM) with myoglobin (Mb) was investigated by UV absorption and fluorescence spectra in combination with molecular modeling under the simulated physiological conditions. The results revealed that the binding site number and apparent binding constant were 1 and 5.27×104 L•mol－1, respectively. Furthermore, molecular modeling results indicated that PM could bind to the site 1 of Mb. Hydrophobic interaction, hydrophilic interaction, hydrogen bond formation and electrostatic interaction could account for the binding of PM. The hydrophobic interactions between the PM and Trp, Tyr, Phe of Mb lead to decrease of UV absorption and fluorescence quenching. Negative value of Δ shows that the binding reaction is thermodynamically favorable.

Key words: phentolamine mesylate (PM), myoglobin (Mb), interaction, molecular modeling