Abstract
The antibacterial target, enoyl-acyl carrier protein (ACP) reductase, is a homotetrameric enzyme that catalyzes the last reductive step of fatty acid biosynthesis. In the present paper, Surflex docking has been carried out on a series (17 compounds) of enoyl ACP reductase inhibitors, using the SYBYL-X 2.0 package (Tripos Inc., St. Louis, USA). Surflex-docking studies revealed that the carboxamide linkage was significant for binding to the receptor, and it is also found that the pattern of binding of tested compounds is same as that of the 2H7M ligand, this in turn helped to understand the specific activity of compounds. The main outcome of this study states that which functional group is responsible for binding with the amino acid at the active site of the enzyme and also tells what type of modification to be done to get even better interaction and binding at the active site of the enzyme.
