Inflammation is a protective mechanism of the human body and is an imperative essential process for the existence of life. However, enhanced inflammatory responses often precipitate unwanted chemical reactions which ultimately results in the aggravation of disease conditions like arthritis, bronchial asthma, inflammatory bowel disease (IBD), etc. The current research involved a Maestro 9.1 software (Glide module) assisted molecular docking study of two pyran non steroidal anti-inflammatory candidates (NSAIC); 2-(but-3-en-1-yl)-5-nonyltetrahydro-2H-pyran (1) and 5-(7-butoxydodecyl)-2-(2-ethylbut-3-en-1-yl)-3,6-dihydro-2H-pyran (2) against anti-inflammatory target 5-LOX (PDB ID: 1N8Q) to determine the potential of experimental molecules. Both the structures had exactly the same Glide score of -5.47 Kcal/mol. It was found that both the compounds 1 and 2 binds perfectly by forming hydrogen bonding with the polar amino acid residues; Gln 514 and Asn 554. The Van der Waals contacts of structure 1 and 2 were found to be 1603 and 1736, respectively, which represented high structural stability to the protein-ligand complex. The structure 1 formed hydrogen bonding with the oxygen atom present in the pyran ring whereas the structure 2 made hydrogen bonding with the oxygen atom present in the chain and the water molecule present in the protein. The studies have also shown that the inhibitors bind firmly to the open cavity and may thus prevent the access of the substrate to the catalytic site of 5-LOX.
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