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- W2056570094 abstract "A range of novel 3-hydroxypyridin-4-ones with different R2 substitutents has been synthesized for the investigation of the structure−activity relationship between the chemical nature of the ligand and the inhibitory activity of the iron-containing metalloenzyme 5-lipoxygenase. Results indicate that the molecular dimensions, together with the lipophilicity, have a critical impact on the ability of this class of chelator to inhibit 5-lipoxygenase. Hydrophilic ligands with a bulky R2 substitutent tend to be weak inhibitors; thus 1,6-dimethyl-2-(4‘-N-n-propylsuccinamido)methyl-3-hydroxypyridin-4(1H)-one (22b) which has the largest R2 substitutent only caused 2% inhibition of the enzyme activity after 30 min incubation at 110 μM IBE (iron-binding equivalents), as compared with deferiprone which caused 40% inhibition of the enzyme activity, under the same conditions." @default.
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- W2056570094 date "2002-01-01" @default.
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- W2056570094 title "Design, Synthesis, and Evaluation of Novel 2-Substituted 3-Hydroxypyridin-4-ones: Structure−Activity Investigation of Metalloenzyme Inhibition by Iron Chelators" @default.
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- W2056570094 doi "https://doi.org/10.1021/jm010817i" @default.
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