食品科学 ›› 2013, Vol. 34 ›› Issue (7): 20-23.doi: 10.7506/spkx1002-6630-201307005

• 基础研究 • 上一篇    下一篇

表没食子儿茶素没食子酸酯与猪胰脂肪酶的相互作用

范志飞,曾维才,戴吉领,何 强*   

  1. 四川大学轻纺与食品学院,四川 成都 610065
  • 收稿日期:2012-02-16 修回日期:2013-03-01 出版日期:2013-04-15 发布日期:2013-03-20
  • 通讯作者: 何 强 E-mail:heq361@163.com
  • 基金资助:
    国家自然科学基金项目(NSFC-31171656)

Interaction of Epigallocatechin-3-gallate with Porcine Pancreas Lipase

FAN Zhi-fei,ZENG Wei-cai,DAI Ji-ling,HE Qiang*   

  1. College of Light Industry, Textile and Food Engineering, Sichuan University, Chengdu 610065, China
  • Received:2012-02-16 Revised:2013-03-01 Online:2013-04-15 Published:2013-03-20
  • Contact: HE Qiang E-mail:heq361@163.com

摘要: 通过荧光光谱法研究表没食子儿茶素没食子酸酯(EGCG)与猪胰脂肪酶(PPL)的相互作用,并基于分子对接技术对其作用机理进行探讨。结果表明:EGCG对PPL具有较强的荧光猝灭作用,并抑制其催化活性,而金属离子(Ca2+、Mg2+、Cu2+、Fe2+)能减弱EGCG对PPL活性的抑制。分子对接研究表明,EGCG可通过疏水键、氢键及Pi-Pi堆积作用与PPL结合,阻碍底物进入酶活中心,从而抑制其活性。

关键词: 表没食子儿茶素没食子酸酯, 猪胰脂肪酶, 荧光猝灭, 分子对接

Abstract: The interaction between epigallocatechin-3-gallate (EGCG) and porcine pancreas lipase (PPL) was studied by fluorescence spectroscopy, and the mechanism was investigated according to molecular docking. Results showed that EGCG could quench PPL fluorescence and inhibit its catalytic activity, while the inhibition was weakened in the presence of Ca2+, Mg2+, Cu2+ or Fe2+. Molecular docking suggested that EGCG might be bound to PPL through hydrophobicity, hydrogen bonds and Pi-Pi interaction, and blocked the entry of substrate into the active center, thus inhibiting the catalytic activity of PPL.

Key words: epigallocatechin-3-gallate, porcine pancreas lipase, fluorescence quenching, molecular docking

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