title: A Molecular Docking and Dynamics Study to Screen Potent Anti-Staphylococcal Compounds Against Ceftaroline Resistant MRSA.
abstract: World Health Organization reports that methicillin-resistant Staphylococcus aureus (MRSA) is the origin of higher proportion of hospital acquired infections. In order to combat the effect of MRSA infection, an ideal drug should stimulate the allosteric exposure of active site, prompting penicillin binding proteins (PBP2a) to bind with that particular compound. Ceftaroline shows high binding affinity towards PBP2a and also confers resistance against degrading enzymes. Recently, two amino acid alterations in the allosteric site of PBP2a, asparagine (N) to lysine (K) at position 146 and glutamic acid (E) to lysine at position 150 are reported to confer resistance against ceftaroline resulting in the rise of ceftaroline-resistant MRSA strains. The present study focuses on the identification of potential ligands that can effectively bind with allosteric site of PBP2a, that leads to the access of active site and entry of a β-lactam antibiotic for effective inhibition. The results obtained from our study will be useful for designing effective compounds with potential therapeutic effects against ceftaroline resistant MRSA strains.
authors.affiliation: Medical & Biological Computing Laboratory, School of Biosciences and Technology, VIT University, Vellore, 632014, Tamil Nadu, India.
authors.forename: P
authors.initials: P
authors.lastname: Lavanya
authors.affiliation: Medical & Biological Computing Laboratory, School of Biosciences and Technology, VIT University, Vellore, 632014, Tamil Nadu, India.
authors.forename: Sudha
authors.initials: S
authors.lastname: Ramaiah
authors.affiliation: Medical & Biological Computing Laboratory, School of Biosciences and Technology, VIT University, Vellore, 632014, Tamil Nadu, India.
authors.forename: Anand
authors.initials: A
authors.lastname: Anbarasu
mesh_terms: D000900:Anti-Bacterial Agents / Q000737:chemistry*; D006860:Hydrogen Bonding; D055624:Methicillin-Resistant Staphylococcus aureus / Q000201:enzymology*; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D046915:Penicillin-Binding Proteins / Q000737:chemistry*; D011485:Protein Binding
chemical_list: D000900:Anti-Bacterial Agents; D046915:Penicillin-Binding Proteins
keywords: ANTI-MRSA COMPOUNDS; LIGANDS; MOLECULAR DYNAMICS; RESISTANCE