您好，欢迎访问上海市农业科学院 机构知识库！
上海市农业科学院机构知识库

全部

  • 全部
  • 标题
  • 学者
  • 机构
  • 关键词

Structural characterization and angiotensin-converting enzyme (ACE) inhibitory mechanism of Stropharia rugosoannulata mushroom peptides prepared by ultrasound

文献类型： 外文期刊

作者： Li, Wen 1 ; Chen, Wanchao 2 ; Ma, Haile 1 ; Wu, Di 2 ; Zhang, Zhong 2 ; Yang, Yan 2 ;

作者机构： 1.Jiangsu Univ, Sch Food & Biol Engn, Inst Food Phys Proc, Zhenjiang 212013, Jiangsu, Peoples R China

2.Shanghai Acad Agr Sci, Natl Engn Res Ctr Edible Fungi, Inst Edible Fungi,Minist Agr, Key Lab Edible Fungi Resources & Utilizat South, Shanghai 201403, Peoples R China

关键词： Stropharia rugosoannulata mushroom; Peptide distribution; Structural characteristics; Formation path; Molecular docking; ACE inhibition mechanism

期刊名称：ULTRASONICS SONOCHEMISTRY （ 影响因子：9.336； 五年影响因子：8.772 ）

ISSN： 1350-4177

年卷期： 2022 年 88 卷

页码：

收录情况： SCI

摘要： To reveal the structural characteristics and angiotensin-converting enzyme (ACE) inhibition mechanism of Stropharia rugosoannulata mushroom peptides prepared by multifrequency ultrasound, the peptide distribution, amino acid sequence composition characteristics, formation pathway, and ACE inhibition mechanism of S. rugosoannulata mushroom peptides were studied. It was found that the peptides in S. rugosoannulata mushroom samples treated by multifrequency ultrasound (probe ultrasound and bath ultrasound mode) were mainly octapeptides, nonapeptides, and decapeptides. Hydrophobic amino acids were the primary amino acids in the peptides prepared by ultrasound, and the amino acid dissociation of the peptide bonds at the C-terminal under the action of ultrasound was performed mainly to produce hydrophobic amino acids. Pro and Val (PV), Arg and Pro (RP), Pro and Leu (PL), and Asp (D) combined with hydrophobic amino acids were the characteristic amino acid sequence basis of the active peptides of the S. rugosoannulata mushroom. The docking results of active peptides and ACE showed that hydrogen bond interaction remained the primary mode of interaction between ACE and peptides prepared by ultrasound. The peptides can bind to the amino acid residues in the ACE active pocket, zinc ions, or key amino acids in the domain, and this results in inhibition of ACE activity. Cation-pi interactions also played an important role in the binding of mushroom peptides to ACE. This study explains the structural characteristics and ACE inhibition mechanism used by S. rugosoannulata mushroom peptides prepared by ultrasound, and it will provide a reference for the development and application of S. rugosoannulata mushroom peptides.

  • 相关文献
作者其他论文 更多>>
置顶
购物车
反馈

© 京ICP备09089781号-29 主办单位：上海市农业科学院

学术资源： 中国农业科学院 农业专业知识服务系统 农科联盟资源共建共享平台 中国农业科技文献与信息服务平台 中国农业期刊集成服务平台