Most varieties of E. coli are harmless or cause relatively brief diarrhea. In contrast, the other strains that cause intestinal sickness. In E. coli, a number of anti-microbial targets have been identified by the researchers, from which fatty acid metabolism protein (FadR) is an emerging and attractive biological target to develop drug candidates. The FadR protein of E. coli has been shown to play a dual role in the transcription of the genes of bacterial fatty acid metabolism. Inhibition of E. coli FadR represents an effective way of controlling the infection. The present investigation involved in silico structure-based drug design (SBDD) screening of two chromene based molecules; (2R)-3-((9S,10aS,10bS)-9-isopropyl-4a,5,6,8,9,10,10a,10b-octahydro-2H-benzo[h]chromen-4-yl)-2-methylpropyl benzoate (1) and (4aR,6R,8R,8aS)-methyl-8-(2-(benzoyloxy)ethyl)-4-((E)-pent-2-en-1-yl)-4a,5,6,7,8,8a-hexahydro-2H-chromene-6-carboxylate (2) as E. coli FadR inhibitors by employing induced-fit docking technique using the Maestro 9.1 software. The present study involved identification of new chromene based compounds as potent anti-bacterial or more specific anti E. coli agents. It was clear from this research that both the compounds perfectly bound with the active site cavity of the biological target. The inhibitors demonstrated hydrogen bonding interactions directly as wells as through water molecules with the amino acid residues, and thus they could penetrate deeper into the active site cavity. These may provide the compounds a better orientation and can inhibit them complementary to the active site. Therefore, the research will undeniably motivate the modern day (medicinal) chemists and biologists to further explore and study the better halves of applications.
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