Journal of Bioequivalence & Bioavailability

Molecular modelling studies of Oxazolidinone antibiotics in E.Coli ribosome

3^rd World Congress Bioavailability & Bioequivalence

March 26-28, 2012 Marriott Hotel & Convention Centre, Hyderabad, India

Naresh Panigrahi, Swastika Ganguly and Jagadeesh Panda

Posters: J Bioequiv Availab

Abstract:

P rotein- Ligand docking has been used as an important tool in computer aided drug design and inhibitor design. The ribosome represents a major target for antibacterial drugs. Being a complex molecular machine, it offers many potential sites for functional interference. The high-resolution structures of ribosome in complex with various antibiotics provide a unique data set for understanding the universal features of drug-binding pockets on the ribosome. With the objective to design new chemical entities with enhanced inhibitory potencies against gram positive bacteria and multidrug resistant organisms. This study was designed to explore binding affinity and antibacterial activity of some newly synthesized 3,5-disubstituted oxazolidinone analogs in to the peptidyl transferase center of E.coli ribosome which was built from Schuwirth et al by using molecular modeling software Glide v 5.0 and the hydrogen-bonding interactions were observed between the inhibitors and the target ribosome. The structure-based drug design strategy described in this study will be highly useful for the development of new inhibitors with high potency and selectivity. From the docking result we can conclude that 3,5-disubstituted oxazolidinone analogs have showed good binding affinity towards the E.coli ribosome