| Popis: |
Background: Methicillin-resistant Staphylococcus aureus (MRSA) contagion is raising serious concerns about dairy cattle. One successful approach to treat MRSA infection is that the potential drug candidate should excite the allosteric view of active site, and form a stable interaction with the penicillin binding proteins (PBP2a), tyrosyl t-RNA synthetase (TyrRs) and thymidylate kinase (TMK) causing cell lysis and bacterial cell death. Objectives: The aims of current study is the identification of a promising active drug molecule which can serve as a ligand for successful inhibition of S. aureus bacterial protein. Methods: 1,7-bis(4-hydroxy-3-methoxy phenoxy)-1,2,6,7- tetraiodoheptane-3,5-dione is an iodinated curcumin, which displayed a stable hydrophobic interaction (docking score~ -8.45 kcal/mol) with the allosteric binding site of PBP2a as compared to ‘curcumin’ (-7.10 kcal/mol) in addition to S. aureus TyrRs and TMK protein. Results: Moreover, the results were cross validated with Hex8.0 program. Molecular simulations studies were also conducted using SwissDock molecular docking program and Autodock Tools-1.5.6. The RMSD plot produced from the simulation study depicted minimum deviation per residue of protein and the deviation was found to be in the range of 0.12 to 1.02Å. Iodinated curcumin demonstrated Minimum Inhibitory Concentration (MIC) values at 60 and 80-μg/ml remarkably lower (P Conclusion: In conclusion, iodinated curcumin deserves further in vivo anti-bacterial analysis as a potential treatment regimen against resistant MRSA strains in dairy cattle mastitis. |
