The LOXs converts arachidonic acid into thromboxane family, which are the most potent inflammatory and allergic mediator and enhances inflammatory responses and often precipitate unwanted chemical reactions which ultimately results in the aggravation of disease conditions like arthritis, bronchial asthma, inflammatory bowel disease (IBD), etc. In such an expedition, the ability of heterocycle pyran in inhibiting the LOX has been explored sensibly. The present research deals with the in-silico molecular docking based screening of two 2-substituted pyran molecules; (R)-2-(but-3-enyl)-tetrahydro-2H-pyran (1) and (R)-2-((S)-2-ethylbut-3-enyl)-3,6-dihydro-2H-pyran (2) against anti-inflammatory target activity LOX by utilizing Glide module of Maestro 9.1 software. A good molecular docking at the active site of 5-LOX was demonstrated where the ligands interacted with the enzymatic target with nearly identical dock Glide score of -6.92 Kcal/mol (1) and -7.17 Kcal/mol (2), respectively along with Van der Waals interactions of 953 and 1048. It was evident that both the pyran compounds formed a single stable hydrogen bonding via oxygen moiety with the polar amino acid residue Gln514 present in the active site cavity of 5-LOX. This study will be really being useful to the researchers across the globe who is working in the direction of inflammatory inhibitor development.
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