Tetrahydroaminoacridine affects the cholinergic function of blood-brain barrier

Catalán, Rosa; Martı́nez, Ana M.; Aragonés, M.D.; Miguel, B.G.; Hernández, Félix; Cruz, Elba de la

doi:10.1016/0024-3205(93)90553-f

Cited by 3 publications

(1 citation statement)

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“…All compounds presented a similar arrangement within the active site of AChE, interacting mainly with the catalytic site ( Figure 5). They mimicked the binding mode of tacrine that is a mixed-type, reversible inhibitor of cholinesterase that binds close to the catalytically active serine in the active site of the enzyme [47]. The benzimidazole ring interacted by π-π stacking with the side chains of Phe330 and Trp84.…”

Section: Molecular Modeling Studiesmentioning

confidence: 97%

Biological Evaluation, Molecular Docking, and SAR Studies of Novel 2-(2,4-Dihydroxyphenyl)-1H- Benzimidazole Analogues

et al. 2019

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In the present study, new 4-(1H-benzimidazol-2-yl)-benzene-1,3-diols, modified in both rings, have been synthesized and their efficacies as acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) inhibitors have been determined.The modified Ellman's spectrophotometric method was applied for the biological evaluation. The compounds showed strong (IC 50 80-90 nM) AChE and moderate (IC 50 5-0.2 µM) BuChE inhibition in vitro. Some compounds were effective toward AChE/BuChE, exhibiting high selectivity ratios versus BuChE, while the other compounds were active against both enzymes. The structure-activity relationships were discussed. The compounds inhibited also in vitro self-induced Aβ(1-42) aggregation and exhibited antioxidant properties. The docking simulations showed that the benzimidazoles under consideration interact mainly with the catalytic site of AChE and mimic the binding mode of tacrine.

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Section: Molecular Modeling Studiesmentioning

confidence: 97%