In silico Identification of Potential Human Acetylcholinesterase Inhibitors from the Nigella sativa Phytochemicals

Acetylcholinesterase degrades the neurotransmitter acetylcholine in nervous system synapses to regulate neurotransmission. It has been demonstrated to be effective as a therapeutic target as well as a target for Alzheimer’s disease drugs. Primary phytoconstituents components of Nigella sativa were identified in this study based on their affinity for an active site binding of Human Acetylcholinesterase. Molecular dynamics and molecular docking methods were used to test the stability of the topmost docking complex. Out of the nine phytochemicals studied in this study, three molecules, Dithymoquinone, Nigellicine, and Nigellidine, were found to have a significant docking score. Based on our findings, Dithymoquinone is the most potent inhibitor of Human Acetylcholinesterase. It is the least energetic protein (10.1 Kcal/mol), resulting in the highest binding affinity. Molecular dynamics studies confirmed the stability of the Dithymoquinone-Human Acetylcholinesterase complex.