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

机构：[1] Institute of Food and Drug Manufacturing Engineering, Guizhou Institute of Technology, Guiyang, 550025, China; [2] Department of Ecology and Resource Engineering, Hetao College, Bayannur, Inner Mongolia, 015000, China; [3] Key Laboratory of Bio-resources and Eco-environment, Ministry of Education, College of Life Sciences, Sichuan University, Chengdu, 610064, China

第一机构：贵州理工学院

通信机构：Key Laboratory of Bio-resources and Eco-environment, Ministry of Education, College of Life Sciences, Sichuan University, Chengdu, 610064, China

年份：2021

卷号：2021

外文期刊名：Journal of Spectroscopy

收录：EI(收录号：20220211453522);Scopus(收录号：2-s2.0-85122493666)

语种：英文

外文关键词：Van der Waals forces - Dichroism - Fluorescence - Binding energy - Hydrogen bonds - Free energy - Molecular dynamics - Hydrophobicity

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 105 mol/L. Thermodynamic parameters (ΔH = 15.76 kJ/mol and ΔS = 158.36 J/mol·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. ? 2021 GuoFei Zhu et al.