Inhibition of Human 5-Lipoxygenase by 3-Nitro-2, 4, 6-trihydroxybenzamide Derivatives

Abstract

The inhibitory effects of 3-nitro-2, 4, 6-trihydroxybenzamide derivatives on human 5-lipoxygenase (5-LO), a key enzyme in arachidonic acid cascades, were examined using 5-LO produced by Escherichia coli. Some of the tested compounds inhibited the conversion of arachidonic acid to 5-hydroperoxy-6, 8, ll, 14-eicosatetraenoic acid (5-HPETE), and in particular the N-phenylbutyl derivative was about 30 times more active (IC₅₀ = 35μM) than caffeic acid (IC₅₀ = 1000 μM), a known selective 5-LO inhibitor.