It is well documented that mammalian lipoxygenases (LOs) are non-heme iron-containing enzymes responsible for the oxidation of polyunsaturated fatty acids and esters to hydroperoxy derivatives [1]. Recently, 15-lipoxygenase has emerged as an attractive target for therapeutic intervention. In addition, the immediate products of 15-LO oxidation of AA and linoleic acid have been shown to be pro-inflammatory and pro-thrombotic [2]. There is reasonable homology between the soybean lipoxygenase(SLO) and the human one [3]. Obviously soybean enzyme is much more accessible than the human one. Therefore, one can expect that the results can be extendable to the human LO. Recently we reported the results of a comparative study on SLO inhibitory activities of eugenol, eugenyl benzoate, methyleugenol and esteragol. Also, we suggested that the inhibitory activity of these molecules largely depends on the orientation of allyl group towards chelated Fe3+-OH and the molecular volume of carboxylate moiety in active site pocket of the enzyme without hydroperoxidation of allylic carbons. In this work, we decided to demethylateesteragol and synthesize the benzoate ester and study its inhibitory potency. Based on the IC50 of this ester comparing to eugenyl benzoate, it is suggested that the methoxy group of eugenyl benzoate have no effective role in inhibitory potency. Then the allyl group of this compound was replaced with allyloxy to study its inhibitory potency. The results of docking analysis showed these compounds have the similar estimated inhibitory constant (Ki) in a range of 2–4 × 106.

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