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Determinants of Adenosine A 2A Receptors‐Perfluoroalkyl Sulfonates Complex: Multi‐Spectroscopic and Molecular Dynamics Simulation Study
Author(s) -
Huang Manting,
Yong Li,
Xu Jie,
Zuo Yanqiu,
Yi Zhongsheng,
Liu Hongyan
Publication year - 2021
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.202100863
Subject(s) - van der waals force , fluorescence , molecular dynamics , chemistry , computational chemistry , molecule , physics , organic chemistry , optics
In this study, we determined the binding characteristics of perfluoroalkyl sulfonates (PFSAs) to the adenosine A 2A receptor (A 2A R) using various spectroscopic methods and computer simulation technologies. UV‐absorption, fluorescence spectra, and three‐dimensional fluorescence spectra results revealed the changes in the micro‐environment of the secondary structure of A 2A R. By comparing the fluorescence spectroscopy of A 2A R in the absence and presence of PFSAs, we found that PFSAs induced the static fluorescence quenching of A 2A R. The thermodynamic parameters ▵ H and ▵ S indicated that van der Waals forces and electrostatic interactions predominantly stabilized the pollutant‐protein system. A molecular dynamics (MD) simulation study of the A 2A R and A 2A R‐PFSAs complex shows that A 2A R‐PFSAs are stable. This study describes the binding mechanism of PFSAs to A 2A R, which is very helpful in improving our understanding of the effect of PFSAs on peripheral tissues and the central nervous system.