ArticleJournal of enzyme inhibition and medicinal chemistry2018
Identification of new allosteric sites and modulators of AChE through computational and experimental tools.
Article in Journal of enzyme inhibition and medicinal chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 50 citations in OpenAlex.
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- Computer-aided Drug Design for Alzheimer's Disease: Recent Advancements and Future Perspectives.Current topics in medicinal chemistry · 2026Review
- Therapeutic potential ofFrontiers in behavioral neuroscience · 2026Article
- New Mannich-type arylidenerhodanines as potent inhibitors of AChE and BChE: synthesis, biological evaluation, cytotoxicity and molecular modeling.RSC advances · 2025Article
- Synthesis, Characterization, and Biological Effects of Chloro-Cathinones: Toxicity and Potential Neurological Impact.International journal of molecular sciences · 2025Article
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- In silico analysis of the use of solanine derivatives as a treatment for Alzheimer's disease.Heliyon · 2024Article
- Patterning amyloid-β aggregation under the effect of acetylcholinesterase using a biological nanopore - anSensors and actuators reports · 2023Article
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- Anticholinesterase and Serotoninergic Evaluation of Benzimidazole-Carboxamides as Potential Multifunctional Agents for the Treatment of Alzheimer's Disease.Pharmaceutics · 2023Article
- A noncommutative combinatorial protein logic circuit controls cell orientation in nanoenvironments.Science advances · 2023Article
- A Comprehensive Review of Cholinesterase Modeling and Simulation.Biomolecules · 2021Review
- CTLA-4 in Regulatory T Cells for Cancer Immunotherapy.Cancers · 2021Review
- Neuroactive venom compounds obtained fromThe journal of venomous animals and toxins including tropical diseases · 2021Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Allosteric sites on proteins are targeted for designing more selective inhibitors of enzyme activity and to discover new functions. Acetylcholinesterase (AChE), which is most widely known for the hydrolysis of the neurotransmitter acetylcholine, has a peripheral allosteric subsite responsible for amyloidosis in Alzheimer's disease through interaction with amyloid β-peptide. However, AChE plays other non-hydrolytic functions. Here, we identify and characterise using computational tools two new allosteric sites in AChE, which have allowed us to identify allosteric inhibitors by virtual screening guided by structure-based and fragment hotspot strategies. The identified compounds were also screened for in vitro inhibition of AChE and three were observed to be active. Further experimental (kinetic) and computational (molecular dynamics) studies have been performed to verify the allosteric activity. These new compounds may be valuable pharmacological tools in the study of non-cholinergic functions of AChE.
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