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A number of penicillin derivatives  (4a-h)  were synthesized by the condensation of 6-amino penicillinic acid (6-APA) with non-steroidal anti-inflammatory drugs as antimicrobial agents.  In silico  docking study of these analogues was performed against Penicillin Binding Protein (PDBID 1CEF) using AutoDock Tools 1.5.6 in order to investigate the antimicrobial data on structural basis. Penicillin binding proteins function as either transpeptidases or carboxypeptidases and in few cases demonstrate transglycosylase activity in bacteria. The excellent antibacterial potential was depicted by compounds  4c  and  4e  against  Escherichia coli ,  Staphylococcus epidermidus  and  Staphylococcus aureus  compared to the standard amoxicillin. The most potent penicillin derivative  4e  exhibited same activity as standard amoxicillin against  S .  aureus . In the enzyme inhibitory assay the compound  4e  inhibited  E .  coli  MurC with an IC 50  value of 12.5 μM. The docking scores of these compounds  4c  and  4e  also verified their greater antibacterial potential. The results verified the importance of side chain functionalities along with the presence of central penam nucleus. The binding affinities calculated from docking results expressed in the form of binding energies ranges from -7.8 to -9.2kcal/mol. The carboxylic group of penam nucleus in all these compounds is responsible for strong binding with receptor protein with the bond length ranges from 3.4 to 4.4 Ǻ. The results of present work ratify that derivatives  4c  and  4e  may serve as a structural template for the design and development of potent antimicrobial agents.

Novel Penicillin Analogues as Potential Antimicrobial Agents; Design, Synthesis and Docking Studies