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Int. J. Mol. Sci. 2015, 16(7), 14786-14807; doi:10.3390/ijms160714786

Characterization of the Interaction between Gallic Acid and Lysozyme by Molecular Dynamics Simulation and Optical Spectroscopy

1
School of Science, Zhejiang Agricultural & Forestry University, Lin'an 311300, China
2
Research Center of Medical Chemistry & Chemical Biology, Chongqing Technology and Business University, Chongqing 400067, China
*
Author to whom correspondence should be addressed.
Academic Editor: Christo Z. Christov
Received: 21 March 2015 / Revised: 8 June 2015 / Accepted: 17 June 2015 / Published: 1 July 2015
(This article belongs to the Section Physical Chemistry, Theoretical and Computational Chemistry)
View Full-Text   |   Download PDF [2216 KB, uploaded 1 July 2015]   |  

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. View Full-Text
Keywords: gallic acid; lysozyme; molecular dynamics simulation; spectroscopic techniques; MM-PBSA method gallic acid; lysozyme; molecular dynamics simulation; spectroscopic techniques; MM-PBSA method
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Zhan, M.; Guo, M.; Jiang, Y.; Wang, X. Characterization of the Interaction between Gallic Acid and Lysozyme by Molecular Dynamics Simulation and Optical Spectroscopy. Int. J. Mol. Sci. 2015, 16, 14786-14807.

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