ArticleAntioxidants (Basel, Switzerland)2026
Structural Insights into the Interaction of Human ALOX15 with the Natural Antioxidant Nordihydroguaiaretic Acid: Functional Inhibitor Studies and Molecular Dynamics Simulations.
Article in Antioxidants (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- A molecular modeling and machine learning-based approach for the identification of potential human ALOX15 inhibitors.Journal of molecular modeling · 2026Article
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6 authors.
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Abstract
Mammalian arachidonic acid lipoxygenases (ALOXs) are lipid-peroxidizing enzymes, which have been implicated in inflammatory, hyperproliferative and neurodegenerative diseases. Nordihydroguaiaretic acid (NDGA) is a naturally occurring antioxidant and a potent lipoxygenase inhibitor. Unfortunately, the molecular basis of the NDGA-ALOX interaction remains unexplored. Here, we show by in silico docking studies and by molecular dynamics simulations that NDGA binds in the substrate binding pocket of human ALOX15 and that Gln595 plays a major role in this interaction. In silico mutagenesis studies (Glu595Ala, Glu595Leu, Glu595Glu, Glu595Ile) modified the stability of the ALOX15-NDGA complex and altered the ligand binding behavior of the enzyme. To validate the in silico findings, we expressed human ALOX15 and the enzyme mutants as recombinant proteins, characterized their functional properties and quantified the IC
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