Here, we report the synthesis, characterization, and biological activities of a series of benzimidazolium salts bearing the trifluoromethylbenzyl group. All benzimidazolium salts were characterized by using nuclear magnetic resonance (NMR) ( 1 H NMR and 13 C NMR), Fourier transform-infrared spectroscopy, and elemental analysis techniques. The crystal structures of some of these compounds were obtained by the single-crystal X-ray diffraction method. Furthermore, the acetylcholinesterase (AChE) and α-glycosidase (α-Gly) enzyme inhibition activities of these compounds were investigated. The obtained results revealed that 2e, with K i value of 1.36 ± 0.34 µM against AChE and 3d with K i value of 91.37 ± 10.38 µM against α-Gly, were the most potent compounds against both assigned enzymes. It should be noted that most of the synthesized compounds were more potent than standard inhibitor tacrine (TAC) against AChE. In silico studies, we focused on compound 2e, 3d, 3e, and 3f as potent inhibitors of AChE and α-Gly, the compound 2e showed good binding energy (−10.23 kcal/mol), among the three selected compounds and positive control (−10.18, −10.08, and −7.37 kcal/mol for 3d, 3f, and TAC, respectively). Likewise, as a result of the same compounds against the α-Gly enzyme, the compound 3d had the highest binding affinity (−8.39 kcal/mol) between the four selected compounds and the positive control (−8.27, −8.10, −8.06, and −7.53 kcal/mol for 3f, 3e, 2e, and acarbose, respectively). From the absorption, distribution, metabolism, excretion, and toxicity analyses, it can be concluded that the compounds under consideration exhibited more drug-likeness properties in the prediction studies compared to positive controls.

The method for producing 4-trifluoromethoxybenzyl substituted benzimidazolium salts is described in this article. The method is based on the reaction of 4-trifluoromethoxybenzyl substituent alkylating agent with 1alkylbenzimidazole. This method yielded 1-(4-trifluoromethoxybenzyl)-3-alkylbenzimidazolium bromide salts. These benzimidazolium salts were characterized by using 1 H-NMR, 13 C-NMR, FT-IR spectroscopy, and elemental analysis techniques. The crystal structure of 1f was enlightened by single crystal X-ray diffraction studies. Also, the enzyme inhibition effects of the synthesised compounds were investigated. They demonstrated highly potent inhibition effect on acetylcholinesterase (AChE) and carbonic anhydrases (hCAs) (K i values are in the range of 7.24 � 0.99 to 39.12 � 5.66 nM, 5.57 � 0.96 to 43.07 � 11.76 nM, and 4.38 � 0.43 to 18.68 � 3.60 nM for AChE, hCA I, and hCA II, respectively). In molecular docking study, the interactions of active compounds showing activity against AChE and hCAs enzymes were examined. The most active compound 1f has À 10.90 kcal/mol binding energy value against AChE enzyme, and the potential structure compound 1e, which has activity against hCA I and hCA II enzymes, was À 7.51 and À 8.93 kcal/mol, respectively.

Herein, we present how to thirteen new synthesize 1-(4-acetylphenyl)-3-alkylimidazolium salts by reacting 4-(1-H-imidazol-1yl)acetophenone with a variety of benzyl halides that contain either electron-donating or electron-withdrawing groups. The structures of the new imidazolium salts were conformed using different spectroscopic method ( 1 H NMR, 13 C NMR, 19 F NMR and FTIR) and elemental analysis techniques. Furthermore, the carbonic anhydrase and acetylcholinesterase enzyme inhibition activities of these compounds were investigated. They showed highly potent inhibition effect toward acetylcholinesterase (AChE) and carbonic anhydrases (hCAs) with K i values in the range of 8.30±1.71 to 120.77±8.61 nM for AChE, 16.97±2.04 to 84.45±13.78 nM for hCA I, and 14.09±2.99 to 69.33±17.35 nM for hCA II, respectively. Most of the synthesized imidazolium salts were appeared to be more potent than the standard inhibitor of tacrine (TAC) against AChE, and Acetazolamide (AZA) against CA. In the meantime, to prospect for potential synthesized imidazolium salt inhibitor(s) against acetylcholinesterase (AChE) and carbonic anhydrases (hCAs), molecular docking and ADMET-based approach was exerted.

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Herein, we present how to thirteen new synthesize 1-(4-acetylphenyl)-3-alkylimidazolium salts by reacting 4-(1-H-imidazol-1-yl)acetophenone with a variety of benzyl halides that contain either electron-donating or electron-withdrawing groups. The structures of the new imidazolium salts were conformed using different spectroscopic method (1H NMR, 13C NMR, 19F NMR and FTIR) and elemental analysis techniques. Furthermore, the carbonic anhydrase and acetylcholinesterase enzyme inhibition activities of these compounds were investigated. They showed highly potent inhibition effect toward acetylcholinesterase (AChE) and carbonic anhydrases (hCAs) with Ki values in the range of 8.30±1.71 to 120.77±8.61 nM for AChE, 16.97±2.04 to 84.45±13.78 nM for hCA I, and 14.09±2.99 to 69.33±17.35 nM for hCA II, respectively. Most of the synthesized imidazolium salts were appeared to be more potent than the standard inhibitor of tacrine (TAC) against AChE, and Acetazolamide (AZA) against CA. In the meantime, to prospect for potential synthesized imidazolium salt inhibitor(s) against acetylcholinesterase (AChE) and carbonic anhydrases (hCAs), molecular docking and ADMET-based approach was exerted.

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