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Phthalimide‐tethered imidazolium salts: Synthesis, characterization, enzyme inhibitory properties, and in silico studies

A series of new imidazolium salts were prepared in good yield by the reaction between 1‐alkylimidazole and a variety of alkyl halides. The structures of the compounds were identified by FT‐IR, 1H NMR, and 13C NMR spectroscopy, elemental analysis, and mass spectrometry. The crystal structure of 1b was determined by the single‐crystal X‐ray diffraction method. The phthalimide‐tethered imidazolium salts exhibited inhibition abilities toward acetylcholinesterase (AChE) and human carbonic anhydrases (hCAs) I and II, with Ki values in the range of 24.63 ± 3.45 to 305.51 ± 35.98 nM for AChE, 33.56 ± 3.71 to 218.01 ± 25.21 nM for hCA I and 17.75 ± 0.96 to 308.67 ± 13.73 nM for hCA II. The results showed that the new imidazolium salts can play a key role in the treatment of Alzheimer's disease, epilepsy, glaucoma, and leukemia, which is related to their inhibition abilities of hCA I, hCA II, and AChE. Molecular docking and in silico absorption, distribution, metabolism, excretion and toxicity studies were used to look into how the imidazolium salts interacted with the specific protein targets. To better visualize and understand the binding positions and the influence of the imidazolium salts on hCA I, hCA II, and AChE conformations, each one was subjected to molecular docking simulations.