Molecular docking simulation of Antibacterial properties of Teixobactin as Bacillus anthracis inhibitor

Anthrax is an acute zoonotic disease caused by Bacillus anthracis. This bacterium is at thetop of the list of dangerous agents for use in biological weapons and bioterrorism. A wide range ofantibiotics are used to treat Anthrax, but usually, treatment may not be effective [۱]. EA۱ is an abundant,highly antigenic, surface-layer protein of Bacillus anthracis vegetative cells [۲]. Teixobactin is apeptide-like secondary metabolite of some species of bacteria that kills some gram-positive bacteria. Itis an inhibitor of cell wall synthesis [۳]. This study aimed to delineate the binding affinity of Teixobactinas EA۱ with Bacillus anthracis inhibitors. The present study used AutoDock Vina, Discovery Studiovisualizer, and MGLTools software for molecular docking and visualization. The crystal structure dataof Acetyl-DELTA۱-۵-Arg۱۰-teixobactin was obtained from the Crystallography Open Database (COD:۷۱۱۹۶۵۸). The crystallographic structure of EA۱ (PDB: ۸OPR) was used from the RCSB protein databank. The binding pocket was calculated by the SCFBio databank. The binding free energy of thestudied compound in the best conformation ΔGbind (kcal/mol) was -۶.۷. The amino acids involved inthe connection site with the studied compound have three residues, including Asn۴۱۹, Tyr۴۲۰, andSer۴۲۲, which form hydrogen bonds in the interaction with the receptor. The findings of this studydemonstrated that the bonding of Teixobactin to the EA۱ protein resulted in a reduction in proteinactivity. Consequently, Teixobactin exhibits potent potential as an antibacterial agent for the treatmentof Anthrax.

کلیدواژه ها:

Molecular docking ، Teixobactin ، Bacillus anthracis ، EA۱