Abstract
The antibacterial target, enoyl-acyl carrier protein (ACP) reductase, is a homotetrameric enzyme that catalyses the last reductive step of fatty acid biosynthesis. In this paper, surflex docking studies have been carried out on a series of 35 pyrrolyl derivatives as enoyl ACP reductase inhibitors. Surflex docking studies revealed that carbonyl, methoxy and nitro group are essential for activity and it showed putative binding modes of the synthesized compounds and it is also found that the pattern of binding of tested compounds is same as that of the 4TZK ligand, this in turn helped in understanding of specific activity of compounds. While the theoretical evaluation of cell permeability based on Lipinski’s rule of five has helped to rationalize the biological results.
