Abstract: This research explores the design, synthesis, and evaluation of benzamide derivatives as inhibitors of acetyl cholinesterase (AChE), a key enzyme involved in the hydrolysis of acetylcholine, a neurotransmitter crucial for cognitive function. The study aims to enhance our understanding of the structure-activity relationships governing the inhibitory potential of these compounds, shedding light on the intricate molecular interactions underlying AChE inhibition. The benzamide derivatives were systematically synthesized and characterized, employing a range of analytical techniques such as spectroscopy and chromatography to confirm their chemical structures and purities. Strategic modifications were introduced during synthesis to optimize the compounds’ inhibitory activity against AChE, with a focus on enhancing potency and selectivity. Molecular docking studies, utilizing computational algorithms and molecular modeling software, provided detailed insights into the binding interactions between the synthesized compounds and the active site of AChE, aiding in the rational design of more effective inhibitors. In vitro experiments, conducted using enzymatic assays and cellular models, demonstrated varying degrees of inhibitory activity across the synthesized compounds, allowing for the identification of lead candidates with the most promising potential for further development as therapeutics for neurodegenerative disorders, such as Alzheimer’s disease. This multidisciplinary approach, combining organic synthesis, computational modeling, and enzymology, represents a concerted effort in drug discovery targeting AChE, with profound implications for the development of innovative treatments addressing the unmet medical needs in neurological disorders.