食品科学 ›› 2022, Vol. 43 ›› Issue (12): 1-6.doi: 10.7506/spkx1002-6630-20210508-081

• 食品化学 •    

EGCG与β-伴大豆球蛋白/大豆球蛋白相互作用对蛋白质结构的影响

黄国,田泽鹏,薛丽莹,陈骐,王迪,衣艳娇,李萌,孙书境,隋晓楠   

  1. (1.东北农业大学食品学院,黑龙江 哈尔滨 150030;2.东北农业大学生命科学学院,黑龙江 哈尔滨 150030)
  • 发布日期:2022-07-01
  • 基金资助:
    国家自然科学基金优秀青年科学基金项目(32022068);国家自然科学基金面上项目(31871809); 东北农业大学SIPT项目(202110224199;202110224032)

Effect of Interaction between EGCG and Soy β-Conglycinin/Glycinin on Protein Structure

HUANG Guo, TIAN Zepeng, XUE Liying, CHEN Qi, WANG Di, YI Yanjiao, LI Meng, SUN Shujing, SUI Xiaonan   

  1. (1. College of Food Science, Northeast Agricultural University, Harbin 150030, China;2. College of Life Sciences, Northeast Agricultural University, Harbin 150030, China)
  • Published:2022-07-01

摘要: 采用荧光光谱、紫外-可见光谱、傅里叶变换红外光谱和分子对接方法,研究中性条件下β-伴大豆球蛋白(β-conglycinin,7S)、大豆球蛋白(glycinin,11S)与表没食子儿茶素没食子酸酯((–)-epigallocatechin-3-gallate,EGCG)的相互作用。结果表明,在中性条件下EGCG与7S/11S蛋白之间存在相互作用,并诱导了氨基酸残基微环境发生变化。EGCG通过动态和静态方式猝灭7S/11S蛋白内源荧光。与7S蛋白相比,EGCG对11S蛋白的亲和力更高。EGCG与7S/11S蛋白的反应自发进行,两者主要通过氢键和范德华力形成物质的量比1∶1的复合物。EGCG能够降低7S/11S蛋白的表面疏水性,并随着EGCG浓度的增加,11S蛋白变化更加明显。傅里叶变换红外光谱和分子对接研究表明除氢键外,疏水相互作用也参与了复合物的形成。EGCG结合导致7S/11S蛋白二级结构发生不同变化,使蛋白质发生解折叠。

关键词: β-伴大豆球蛋白;大豆球蛋白;表没食子儿茶素没食子酸酯;相互作用

Abstract: The interaction between β-conglycinin (7S)/glycinin (11S) and (–)-epigallocatechin-3-gallate (EGCG) under neutral conditions was characterized by fluorescence spectroscopy, ultraviolet-visible (UV-Vis) absorption spectroscopy, Fourier transform infrared (FTIR) spectroscopy and molecular docking. The results showed that EGCG and 7S/11S could interact with each other at pH 7.0, which induced a change in the microenvironment of amino acid residues. EGCG could quench the intrinsic fluorescence of 7S/11S in dynamic and static manners. EGCG had higher affinity to 11S than to 7S. The reaction between EGCG and 7S/11S was a spontaneous binding process, resulting in the formation of a complex at 1:1 molar ratio by hydrogen bonding and van der Waals force. EGCG could reduce the surface hydrophobicity of 7S/11S. With increasing EGCG concentration, 11S showed a greater change in surface hydrophobicity. FTIR and molecular docking studies suggested that in addition to hydrogen bonds, hydrophobic interactions were also involved in the formation of complexes. Binding to EGCG could cause different changes in the secondary structure of 7S/11S subsequently resulting in protein unfolding.

Key words: β-conglycinin (7S); glycinin (11S); (–)-epigallocatechin-3-gallate; interaction

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