文献类型：期刊文献

英文题名：Investigation on the Binding and Conformational Change of All-trans-Retinoic Acid with Peptidyl Prolyl cis/trans Isomerase Pin1 Using Spectroscopic and Computational Techniques

作者：Zhu, GuoFei Lyu, ShaoLi 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 550025, Peoples R China;[2]Hetao Coll, Dept Ecol & Resource Engn, Bayannur 015000, Inner Mongolia, Peoples R China;[3]Sichuan Univ, Coll Life Sci, Minist Educ, Key Lab Bioresources & Ecoenvironm, 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, Minist Educ, Key Lab Bioresources & Ecoenvironm, Chengdu 610064, Peoples R China.

年份：2021

卷号：2021

外文期刊名：JOURNAL OF SPECTROSCOPY

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000737260600001)】；

基金：This work was financially supported by the Science and Technology Foundation of Guizhou Province of China (qian ke he zi [2017]1068) and Guizhou Institute of Technology High-Level Talent Research Startup Project (XJGC20190658).

语种：英文

外文关键词：Binding energy - Dichroism - Fluorescence - Free energy - Hydrogen bonds - Hydrophobicity - Molecular dynamics - Principal component analysis

摘要：Binding and conformational change of all-trans-retinoic acid (ATRA) with peptidyl prolyl cis/trans isomerase Pin1 were investigated systematically by spectroscopic and computational techniques under experimentally optimized physiological conditions. The intrinsic fluorescence of Pin1 was quenched through a static quenching mechanism in the presence of ATRA with binding constants on the order of 10(5) mol/L. Thermodynamic parameters (Delta H = 15.76 kJ/mol and Delta S = 158.36 J/mol center dot K at 293 K) and computational results illustrated that the hydrophobic interactions played a significant role in the binding process of ATRA to Pin1, but electrostatic forces, weak van der Waals, and hydrogen bonds cannot be ignored. Circular dichroism, fluorescence spectra, and computational simulations revealed that ATRA interacted with residues Lys63 and Arg69 of Pin1 to affect its conformational changes. Molecular dynamic simulation, principal component analysis, and free energy landscape monitored the dynamical conformational characteristics of ATRA binding to Pin1. All in all, the present research might provide a reference for the development and design of retinoic acid drugs that inhibit the activity of Pin1.