ANTI-ALCOHOL POTENTIAL OF 1-ARYL-6,7-DIMETHOXY-1,2,3,4-TETRAHYDROISOQUINOLINE DERIVATIVES: IN SILICO MODELING OF INTERACTION WITH ADH ORTHOSTERIC SITES
Abstract
Alcohol dehydrogenase (ADH) is an enzyme involved in ethanol metabolism by catalyzing its oxidation to acetaldehyde. The interaction of 34 derivatives of 1,2,3,4-tetrahydroisoquinoline with the orthosteric sites of alcohol dehydrogenase (PDB ID: 1HDX) were investigated in silico. According to molecular docking results, the investigated ligands exhibited high binding affinity (G) toward the orthosteric sites of alcohol dehydrogenase (PDB ID: 1HDX), forming specific and stable complexes via a non-competitive mechanism. These in silico findings fundamentally support the ligands' capacity to influence ADH conformational stability, thereby modulating the neurotoxic and systemic pharmacological impacts of alcohol at the hepatocyte level.
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