文献类型：期刊文献

英文题名：Spectroscopic and computational studies on the binding interaction between gallic acid and Pin1

作者：Zhu, Guo Fei Lyu, Shao Li Liu, Yang Ma, Chao Wang, Wang

第一作者：朱国飞

通信作者：Wang, W[1]

机构：[1]Guizhou Inst Technol, Inst Food & Drug Mfg Engn, Guiyang, Peoples R China;[2]Hetao Coll, Dept Ecol & Resource Engn, Bayannur, Inner Mongolia, Peoples R China;[3]Sichuan Univ, Coll Life Sci, Key Lab Bioresources & Ecoenvironm, Minist Educ, Chengdu 610064, Peoples R China

第一机构：贵州理工学院

通信机构：corresponding author), Sichuan Univ, Coll Life Sci, Key Lab Bioresources & Ecoenvironm, Minist Educ, Chengdu 610064, Peoples R China.

年份：2021

卷号：36

期号：8

起止页码：2014-2021

外文期刊名：LUMINESCENCE

收录：;EI(收录号：20231713991774);Scopus(收录号：2-s2.0-85116803478);WOS:【SCI-EXPANDED(收录号:WOS:000705100900001)】；

基金：Guizhou Institute of Technology High-level Talent Research Startup Project, Grant/Award Number: XJGC20190658; Science & Technology Foundation of GuiZhou Province of China, Grant/Award Number: qian ke he zi [2017]1068

语种：英文

外文关键词：computational simulation; gallic acid; Pin1; spectra

摘要：Gallic acid (GA) is a natural ingredient in functional foods, which has various health-promoting and antitumour effects. Peptidyl-prolyl cis/trans isomerase Pin1 plays an important role in preventing the development of some malignant tumours. However, whether there was an interaction between Pin1 and GA remains unknown. In this work, the binding information of GA and Pin1 was investigated systematically using multiple spectral and computational methods. GA bound to Pin1 directly with moderate binding affinity in the order of 10(4) mol/L, therefore decreasing the activity of Pin1. Also, the binding process of GA to Pin1 was driven through weak van der Waals forces, hydrogen bonds, and electrostatic forces. In addition, the important residues Lys63, Arg68, and Arg69 played a significant role in maintaining the binding stability between Pin1 and GA. Interestingly, GA reduced the activity of Pin1 by affecting its conformational characteristics. Our present work showed that GA binds to Pin1 and inhibits its activity, affecting its structural and functional properties, which may contribute to the therapy of Pin1-related diseases.