Neutrophil elastase, a serine proteinase from the chymotrypsin family, has been the object of comprehensive experimental and
theoretical studies to develop efficient human neutrophil elastase inhibitors. The serine protease has been linked to the pathology of a variety
of inflammatory diseases, making it an attractive target for the development of anti-inflammatory compounds.
In this work, we have built a common binding model of the 2-pyridin-3-yl-benzo[d][1,3]oxazin-4-one derivatives into the human neutrophil
elastase binding site. This was accomplished through a comparative conformational analysis (using OMEGA, HYPERCHEM, and
MOPAC software) of 2-pyridin-3-yl-benzo[d][1,3]oxazin-4-one inhibitors followed by rigid and flexible molecular docking (by the
FRED and GLIDE programs) into the target protein. We conclude that OMEGA software generates the most representative conformers
to model the protein-ligand interactions.
Keywords: Conformational analysis, Benzoxazinone derivative, Biologically active conformation, Human neutrophil elastase inhibitor, Molecular
docking, serine proteinase, chymotrypsin family, anti-inflammatory compounds, 2-pyridin-3-yl-benzo[d][1, 3]oxazin-4-one derivatives, MOPAC software
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