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Acta Chimica Sinica ›› 2010, Vol. 68 ›› Issue (15): 1494-1498. Previous Articles     Next Articles

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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

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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