高等学校化学学报

高等学校化学学报 ›› 2012, Vol. 33 ›› Issue (05): 1069.doi: 10.3969/j.issn.0251-0790.2012.05.037

• 物理化学 • 上一篇    下一篇

精氨酸酶Ⅰ与丁基苯酞的相互作用

李帅1, 黄旭日1, 赵刚2, 孙若溪2, 高雪峰2   

  1. 1. 吉林大学理论化学研究所, 长春 130021;
    2. 吉林大学生命科学学院, 长春 130012
  • 收稿日期:2011-05-04 出版日期:2012-05-10 发布日期:2012-05-10
  • 作者简介:高雪峰, 男, 博士, 副教授, 主要从事分子生物学模拟研究. E-mail: gaoxf@jlu.edu.cn
  • 基金资助:

    河北省自然科学基金(批准号: C2011319002)资助.

Interaction Between ArginaseⅠand Butylphthalide

LI Shuai1, HUANG Xu-Ri1, ZHAO Gang2, SUN Ruo-Xi2, GAO Xue-Feng2   

  1. 1. Institute of Theoretical Chemistry, Jilin University, Changchun 130021, China;
    2. College of Life Sciences, Jilin University, Changchun 130012, China
  • Received:2011-05-04 Online:2012-05-10 Published:2012-05-10

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被引次数

5

摘要： 利用代谢物组学推测出精氨酸酶Ⅰ作为丁基苯酞的作用靶点的可能性, 然后用分子对接和分子动力学模拟研究了单一手性的左旋(L)和右旋(D)丁基苯酞与精氨酸酶Ⅰ的相互作用, 结果发现, L-丁基苯酞与精氨酸酶Ⅰ形成的复合物比较稳定. 随后的酶学实验也证实, L-丁基苯酞对精氨酸酶Ⅰ有明显的激活作用, 而D-丁基苯酞对其活性无明显影响.

关键词: 精氨酸酶Ⅰ, 丁基苯酞, 手性, 激活剂, 分子动力学

Abstract: Arginase Ⅰ is one of the two subtypes of arginase, mainly exists in the cytoplasm of the liver, brain and other place. Arginine can be metabolized to ornithine, and then ornithine metabolized to polyamines. In this paper it was suggested that arginase Ⅰ might play an role of target for n-butylphthalide(NBP) by metabonomics, and then the interaction between arginase Ⅰ and chiral butylphthalide(L- and D-) was studied via molecular docking and molecular dynamics simulations, and it was found that complex L-NBP-arginase Ⅰ was more stable. The experimental results confirmed that L-NBP has the obvious activation function to arginase Ⅰ, but the D-NBP does not have obvious influence on arginase Ⅰ.

Key words: Arginase Ⅰ, Butylphthalide, Chiral, Activator, Molecular dynamics

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