The bocillin binding assay corroborated the docking analysis. Amongst all the phytochemicals studied, chlorogenic acid (CGA) was found to have highest affinity towards PBP3 TP domain. The phytochemicals exhibiting antibacterial activities were selected as ligands for docking studies employing Schrӧdinger Suite (Maestro, LLC, New York, NY, 2015). coli, a major causative agent of bacterial infection. The current study epitomizes the binding of phytochemicals to the transpeptidation (TP) domain of PBP3 of E. Bioactive phytochemicals from medicinal plants have been proven to reveal important pharmacological and therapeutic properties for developing novel antibacterial agents. Hence, PBPs are the primary targets for developing antibacterial agents as its inhibition leads to irregularities in cell wall structure and eventually cell death. These PBPs are involved in the final stages of peptidoglycan synthesis. The major mechanisms that bacteria evolve to develop resistance against β-lactam class of antibiotics are the production of β-lactamases and expression of low affinity penicillin binding proteins (PBPs).
The extensive and uncontrolled use of antibiotics increases the number of multi drug resistant (MDR) bacterial strains. COLI PBP3: APPROACH TOWARDS NOVEL ANTIBACTERIAL THERAPEUTIC AGENT AbstractĮmergence of antibiotic resistance has become a serious problem worldwide. IN-SILICO DOCKING STUDIES OF PHYTO-LIGANDS AGAINST E.