版权说明 操作指南
首页 > 成果 > 详情

Inhibition and molecular mechanism of diosmetin against xanthine oxidase by multiple spectroscopies and molecular docking

认领
导出
Link by 万方学术期刊
反馈
分享
QQ微信 微博
成果类型:
期刊论文
作者:
Liu, Yongjie;Chen, Hao;Xiang, Huilong;Lei, Huan;Zhang, Di;...
通讯作者:
Xu, Lingyun
作者机构:
[Qin, Yinsheng; Xu, Lingyun; Liu, Yongjie; Xiang, Huilong] Wuhan Polytech Univ, Hubei Key Lab Anim Nutr & Feed Sci, Xuefu South Rd 68, Wuhan 430023, Peoples R China.
[Xu, Lingyun; Liu, Yongjie; Xiang, Huilong; Lei, Huan; Zhang, Di] Wuhan Polytech Univ, Sch Biol & Pharmaceut Engn, Xuefu South Rd 68, Wuhan 430023, Peoples R China.
[Chen, Hao] Wuhan Polytech Univ, Sch Chem & Environm Engn, Wuhan, Peoples R China.
通讯机构:
[Xu, Lingyun] W
Wuhan Polytech Univ, Hubei Key Lab Anim Nutr & Feed Sci, Xuefu South Rd 68, Wuhan 430023, Peoples R China.
Wuhan Polytech Univ, Sch Biol & Pharmaceut Engn, Xuefu South Rd 68, Wuhan 430023, Peoples R China.
语种:
英文
关键词:
Amino acids;Catalysis;Dichroism;Fluorescence;Hydrogen bonds;Molecular modeling;Van der Waals forces;Catalytic functions;Fluorescence titrations;Inhibitory activity;Microenvironments;Molecular docking;Molecular mechanism;Synchronous fluorescence;Ultraviolet absorption spectroscopy;Circular dichroism spectroscopy;allopurinol;diosmetin;hydroxyl group;luteolin;tryptophan;tyrosine;xanthine oxidase;absorption spectroscopy;alpha helix;Article;beta sheet;beta turn;catalysis;circular dichroism;drug efficacy;drug mechanism;fluorescence analysis;hydrogen bond;IC50;in vitro study;molecular docking;priority journal;quorum sensing;spectrofluorometry;titrimetry;ultraviolet visible spectroscopy
期刊:
NEW JOURNAL OF CHEMISTRY
ISSN:
1144-0546
年:
2020
卷:
44
期:
17
页码:
6799-6809
基金类别:
This study was financially supported by the Open Project of Hubei Key Laboratory of Animal Nutrition and Feed Science (Grant No. 201912) and the National Natural Science Foundation of China (Grant No. 31572572). Especially, we are grateful for the help of Ms Yi Tian Yap at the Department of Physiology, Wayne State University, USA for editing this manuscript.
机构署名:
本校为第一且通讯机构
院系归属:
生命科学与技术学院
化学与环境工程学院
动物科学与营养工程学院
摘要:
Diosmetin, as a methoxyflavone compound, was investigated for its interaction and mechanism with xanthine oxidase (XOD), which is a key enzyme catalyzing xanthine to uric acid and finally causing hyperuricemia. Using a kinetic analysis method, diosmetin was shown to possess a strong inhibitory activity for XOD in a reversibly competitive manner with an IC50value of (5.08 ± 0.48) × 10−6mol L−1. The results of fluorescence titrations showed that the combination of diosmetin with XOD gave spontaneous, exothermic static quenching, and hydrogen ...

反馈

验证码:
看不清楚,换一个
确定
取消

成果认领

标题:
用户 作者 通讯作者
请选择
请选择
确定
取消

提示

该栏目需要登录且有访问权限才可以访问

如果您有访问权限,请直接 登录访问

如果您没有访问权限,请联系管理员申请开通

管理员联系邮箱:yun@hnwdkj.com