It is well documented that lipoxygenases (LOs) are non-heme iron-containing enzymes responsible for the oxidation of polyunsaturated fatty acids and esters to hydroperoxy derivatives. Among the mammalian lipoxygenases involved in the etiology of human disease, 5-lipoxygenase (5-LO) is now well established as a target for reducing the production of leukotrienes [1]. More recently, 15-lipoxygenase (15-LO) has emerged as an attractive target for therapeutic intervention.5 15-LO has been implicated in the progression of certain cancers [2] and chronic obstructive pulmonary disease (COPD) [3]. Herein we report a group of 4-allyloxyaniline amides as potential inhibitors of soybean 15-lipoxygenase (SLO). All compounds were docked in SLO active site and showed that allyloxy group of compounds is oriented towards the Fe3+-OH moiety in the active site of enzyme and fixed by hydrogen bonding with two conserved His513 and Gln716. It is resulted that molecular volume of the amide moiety would be a major factor in inhibitory potency variation of the synthetic amides, where the hydrogen bonding of the amide group could also involve in the activity of the inhibitors.

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