title: Characterization of the Interaction between Gallic Acid and Lysozyme by Molecular Dynamics Simulation and Optical Spectroscopy.
abstract: The binding interaction between gallic acid (GA) and lysozyme (LYS) was investigated and compared by molecular dynamics (MD) simulation and spectral techniques. The results from spectroscopy indicate that GA binds to LYS to generate a static complex. The binding constants and thermodynamic parameters were calculated. MD simulation revealed that the main driving forces for GA binding to LYS are hydrogen bonding and hydrophobic interactions. The root-mean-square deviation verified that GA and LYS bind to form a stable complex, while the root-mean-square fluctuation results showed that the stability of the GA-LYS complex at 298 K was higher than that at 310 K. The calculated free binding energies from the molecular mechanics/Poisson-Boltzmann surface area method showed that van der Waals forces and electrostatic interactions are the predominant intermolecular forces. The MD simulation was consistent with the spectral experiments. This study provides a reference for future study of the pharmacological mechanism of GA.
authors.affiliation: School of Science, Zhejiang Agricultural & Forestry University, Lin'an 311300, China. manuscript.usezl@gmail.com.
authors.forename: Minzhong
authors.initials: M
authors.lastname: Zhan
authors.affiliation: School of Science, Zhejiang Agricultural & Forestry University, Lin'an 311300, China. tdky@hotmail.com.
authors.forename: Ming
authors.initials: M
authors.lastname: Guo
authors.affiliation: Research Center of Medical Chemistry & Chemical Biology, Chongqing Technology and Business University, Chongqing 400067, China. ctbujyk@swu.edu.cn.
authors.forename: Yanke
authors.initials: Y
authors.lastname: Jiang
authors.affiliation: School of Science, Zhejiang Agricultural & Forestry University, Lin'an 311300, China. wangxiaomeng0426@163.com.
authors.forename: Xiaomeng
authors.initials: X
authors.lastname: Wang
mesh_terms: D000595:Amino Acid Sequence; D005707:Gallic Acid / Q000737:chemistry* / Q000494:pharmacology; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding
chemical_list: D005707:Gallic Acid; D009113:Muramidase
keywords: MM-PBSA method; gallic acid; lysozyme; molecular dynamics simulation; spectroscopic techniques