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Molecular docking revealed strong binding of polyphenols and vitamins to aflatoxin aldehyde reductase, suggesting potential enzyme modulation.
Aflatoxin aldehyde reductase (AFAR, also known as AKR7A2) is a key member of the aldo-keto reductase superfamily and plays an essential role in cellular defense by reducing toxic aldehyde intermediates generated during aflatoxin B1 metabolism. Targeting the NADPH-binding pocket of AFAR may represent a novel strategy to modulate its detoxification capacity. In this study, we employed molecular docking to evaluate the binding potential of 50 selected natural compounds, including hesperidin, curcumin, rhaponticin, folic acid, and astringin. All tested ligands exhibited strong binding affinities (ΔG ≈ –9.6 to –11.0 kcal/mol), comparable to the native cofactor NADPH (–12.7 kcal/mol). Interaction analysis revealed multiple hydrogen bonds, hydrophobic contacts, and π–π stacking stabilizing the ligand–enzyme complexes. These findings suggest that natural polyphenols and vitamins may effectively compete with NADPH at the AFAR active site, thereby acting as potential modulators of the enzyme’s function. This work offers a computational foundation for future biochemical investigations and underscores the possible therapeutic relevance of these compounds in liver protection and cancer prevention.
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Ivan Vito Ferrari (2025) studied this question.
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