Abstract
Abstract Analogues of tacrine were synthesized and evaluated for acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) inhibitory activity. Compound 2a was the most potent inhibitor of AChE with a higher selectivity than tacrine for AChE over BuChE. Tacrine, on the other hand, showed the opposite behaviour with a weaker inhibitory effect on AChE than on BuChe. The compounds displayed correlated activities in isolated enzymes as well as in rat brain homogenates.
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