Abstract
In response to inflammatory stimuli by bacterial lipopolysaccharide, COX-2 induces the production of prostaglandins and thromboxanes. The Overexpression of COX-2 has been associated with high levels of PGE2 and the modulation of COX-2 and iNOS reduces the inflammation process. The objective of this investigation was to determine the binding mechanism of dibutylphthalate with COX-2 and with mPGES-1.The docking studies were carried out and the inhibitor binding positions and affinity were evaluated using Auto dock 4. We observed that amino acid residues Arg120, Ala527 and Ser530 in COX-2 and Arg38 in mPGES-1 are important for inhibitor recognition via hydrogen bonding interactions.
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