Cholinesterase Inhibition Activity and Molecular Docking Study of Eugenol Derivatives

The study was conducted to explore the anticholinesterase inhibition property of eugenol derived molecules. Ten eugenol derivatives were synthesized and evaluated for the inhibitory activities against acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) by Ellman's method. Most of the tested derivatives showed higher inhibition on BChE than AChE, however, their overall inhibitory activity was weak. In contrast, three derivatives (compounds 3,6,9) showed higher and good AChE inhibitory activity of more than 50% inhibition at 10 mu g/mL. Among them, compound 9 bearing a ethyl substituent at para position of the benzoyl ring showed the most potent AChE inhibition, with IC50 of 5.64 mu g/mL. Ligand-protein docking simulation was also performed for the most active derived molecules (compounds 3,6,9).

Automated summary

The study found that most eugenol derivatives had higher inhibitory activities against butyrylcholinesterase (BChE) compared to acetylcholinesterase (AChE), but their overall inhibitory activity was weak. However, three derivatives showed good AChE inhibitory activity at 10 µg/mL, with compound 9 exhibiting the most potent AChE inhibition with an IC50 of 5.64 µg/mL. Additionally, ligand-protein docking simulation was performed for the most active derived molecules (compounds 3, 6, 9).