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.
Highlights
At present, targeted drug delivery that directly leads to drug delivery to target organs, tissue, and cells is a modern pharmaceutical research hotspot
A synchronous fluorescence spectroscopy and fluorescence phase diagram method showed that the interaction of gallic acid (GA) with LYS affects the conformation of the Trp residue microregion and the conformation change of LYS follows a two-state mode
Molecular dynamics simulations were performed on the GA-LYS complex to investigate the binding mode of the complex
Summary
At present, targeted drug delivery that directly leads to drug delivery to target organs, tissue, and cells is a modern pharmaceutical research hotspot. GA is a natural anticancer drug with many biological activities, such as anti-inflammatory, antitumor, antimutation, and antioxidant [15,16] It is an important organic fine chemical product, which is widely used in agriculture, daily chemical products, food, and paints [16,17]. The binding between GA and LYS was investigated to understand the specific interaction mechanism. The information obtained in this study could help to shed light on the interaction mechanism between GA and LYS. It could guide the design of new drugs for the treatment of a variety of diseases associated with GA [28,29]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
