文献类型：期刊文献

中文题名：Screening of dandelion phenolic extracts and their anti-bacterial function against Escherichia coli through acting on Na^(+)-K^(+) ATPase

作者：Pujun Xie[1,2] Xiang Wang[1,2] Lixin Huang[1,2] Yejun Deng[1,2] Caihong Zhang[1,2]

第一作者：Pujun Xie;谢普军

机构：[1]Institute of Chemical Industry of Forest Products,Chinese Academy of Forestry,National Engineering Laboratory for Biomass Chemical Utilization,Key and Open Laboratory on Forest Chemical Engineering,National Forestry and Grassland Administration,Key Laboratory of Biomass Energy and Material,Number 16 Suojin Wucun,Xuanwu District,Nanjing City,Jiangsu Province 210042,People’s Republic of China;[2]Co-Innovation Center of Efficient Processing and Utilization of Forest Resources,Nanjing Forestry University,Nanjing 210037,China

年份：2024

卷号：6

期号：1

起止页码：327-341

中文期刊名：Food Production, Processing and Nutrition

外文期刊名：食物生产加工与营养(英文)

基金：supported by the National Natural Science Foundation of China[grant no.32271820];the Natural Science Foundation of Jiangsu Province[grant no.BK20181124].

语种：英文

中文关键词：Dandelion organs;Caffeic acid;Membrane leakage;ATPase inhibition;Molecular docking;Molecular dynamics simulation

分类号：TS201.3

摘要：Food contamination by Escherichia coli(E.coli)is an increasing public health concern.Screening for natural plant preservatives has received increasing attention.In this study,dandelion flower phenolic extract(DFPE),with the strongest bacterial inhibition and the highest polyphenol level from various organs,was identified using HPLC and FTIR.The results showed a significant increase in extracellular ATP levels due to cellular membrane leakage in E.coli and decreased Na^(+)-K^(+) ATPase activity.These behaviors were caused by representative phenolic compounds such as caffeic acid in DFPE.Molecular docking simulations were performed to reveal the mechanism of interaction between caffeic acid and Na^(+)-K^(+) ATPase.This indicated that conventional hydrogen bonds,pi-anions,and pi-alkyl were involved in the interaction between them.Molecular dynamic equilibrium of the liganded ATPase complex was achieved after 20 ns.The lower values of Rg and SASA demonstrated that the liganded ATPase structure changed from a relatively loose to a tight state in the presence of caffeic acid.Overall,these findings are meaningful for screening bioactive compounds from various food-derived plant tissues using a combination of practical experimentation and molecular simulations.