Chloro-/fluorobenzyl-substituted benzimidazolium salts were synthesized from the reaction of 4-fluorobenzyl/2-chloro-4-fluorobenzyl-substituted benzimidazole and chlorinated aromatic hydrocarbons. They were characterized using various spectroscopic techniques (Fourier-transform infrared and nuclear magnetic resonance) and elemental analysis. In addition, the crystal structures of the complexes 1a -d and 2b were determined by single-crystal X-ray diffraction methods. These compounds were crystallized in the triclinic crystal system with a P-1 space group. The crystal packing of all complexes is dominated by O-H⋯Cl hydrogen bonds, which link the water molecules and chloride anions, forming a chloride-water tetrameric cluster. These synthesized salts were found to be effective inhibitors for α-glycosidase and acetylcholinesterase (AChE), with K i values ranging from 45.77 ± 6.83 to 102.61 ± 11.56 µM for α-glycosidase and 0.94 ± 0.14 to 10.24 ± 1.58 µM for AChE. AChE converts acetylcholine into choline and acetic acid, thus causing the return of a cholinergic neuron to its resting state. Discovering AChE and α-glycosidase inhibitors is one of the important ways to develop new drugs for the treatment of Alzheimer's disease and diabetes.

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A series of the silver N‐heterocyclic carbene (NHC) complexes have been synthesized from the reactions between benzimidazolium salts bearing fluorinated benzyl group and Ag2O via the deprotonation method. All Ag(I)NHC complexes were characterized by known spectroscopic techniques (1H nuclear magnetic resonance [NMR], 13C NMR, and Fourier transform infrared [FT‐IR]) and elemental analysis. The molecular structures of the two complexes were unambiguously elucidated through single‐crystal X‐ray diffraction analysis. Namely, X‐ray studies show that the coordination geometry around the Ag(I) atom in the case of complex 2c is revealed to be almost linear with C–Ag–Cl angle, whereas in complex 2e, it appears as a nonlinear structure. The inhibitory profiles of these new complexes are investigated on some metabolic enzymes. Representatively, the most potent complex against human carbonic anhydrase isoenzymes I and II (hCAs I and II), 2d, was 1.8 times more potent than standard inhibitor acetazolamide against hCAs I and II. On the other hand, complexes 2c and 2b as most potent compounds against both cholinesterase enzymes was around 5 and 1.6 times more potent than tacrine against acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), respectively. The most active α‐glucosidase inhibitor 2d had similar activity to acarbose as a standard inhibitor. Furthermore, it confirms its in vitro studies as a result of molecular docking studies for each enzyme with (i) binding energy and inhibition constant values and (ii) the definition of the best conformation and nonbonding interactions of the related complexes (2b, 2c, and 2d) against the different target proteins.

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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.

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.