ArticleACS chemical neuroscience2014
Acetylcholinesterase inhibitors with photoswitchable inhibition of β-amyloid aggregation.
Article in ACS chemical neuroscience, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 112 citations in OpenAlex.
- Red-light-activated and thermally-stable amido-dithienylethenes for the reversible control of G-quadruplex binding and anticancer activity.Bioorganic chemistry · 2026Article
- Acetylcholinesterase as a Multifunctional Target in Amyloid-Driven Neurodegeneration: From Dual-Site Inhibitors to Anti-Agregation Strategies.International journal of molecular sciences · 2025Review
- Light-Activated Pharmacological Tools for Exploring the Cholinergic System.Medicinal research reviews · 2025Review
- Synthesis of Bis-Thioacid Derivatives of Diarylethene and Their Photochromic Properties.ACS omega · 2024Article
- Determination of Potential Lead Compound fromInternational journal of molecular sciences · 2024Article
- Recent Progress in Regulating the Activity of Enzymes with Photoswitchable Inhibitors.Molecules (Basel, Switzerland) · 2024Review
- Smart photopharmacological agents: LaVONanoscale advances · 2024Article
- Article
- New cyclopentaquinoline and 3,5-dichlorobenzoic acid hybrids with neuroprotection against oxidative stress for the treatment of Alzheimer's disease.Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Investigation on NovelMolecules (Basel, Switzerland) · 2023Article
- Dual-Acting Small Molecules: Subtype-Selective Cannabinoid Receptor 2 Agonist/Butyrylcholinesterase Inhibitor Hybrids Show Neuroprotection in an Alzheimer's Disease Mouse Model.Journal of medicinal chemistry · 2023Article
- Tacrine-Based Hybrids: Past, Present, and Future.International journal of molecular sciences · 2023Review
- On photokinetics under monochromatic light.Frontiers in chemistry · 2023Article
- Novel benzimidazole-based pseudo-irreversible butyrylcholinesterase inhibitors with neuroprotective activity in an Alzheimer's disease mouse model.RSC medicinal chemistry · 2022Article
- Real-time precision opto-control of chemical processes in live cells.Nature communications · 2022Article
- Design, synthesis and biological evaluation of light-driven on-off multitarget AChE and MAO-B inhibitors.RSC medicinal chemistry · 2022Article
- A DNA-Based Two-Component Excitonic Switch Utilizing High-Performance Diarylethenes.Angewandte Chemie (International ed. in English) · 2022Article
- Steroid-Quinoline Hybrids for Disruption and Reversion of Protein Aggregation Processes.ACS medicinal chemistry letters · 2022Article
- Rational design and synthesis of modified natural peptides from Boana pulchella (anura) as acetylcholinesterase inhibitors and antioxidants.Amino acids · 2022Article
- Photo-Switchable Sulfonylureas Binding to ATP-Sensitive Potassium Channel Reveal the Mechanism of Light-Controlled Insulin Release.The journal of physical chemistry. B · 2021Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Photochromic cholinesterase inhibitors were obtained from cis-1,2-α-dithienylethene-based compounds by incorporating one or two aminopolymethylene tacrine groups. All target compounds are potent acetyl- (AChE) and butyrylcholinesterase (BChE) inhibitors in the nanomolar concentration range. Compound 11b bearing an octylene linker exhibited interactions with both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. Yet upon irradiation with light, the mechanism of interaction varied from one photochromic form to another, which was investigated by kinetic studies and proved "photoswitchable". The AChE-induced β-amyloid (Aβ) aggregation assay gave further experimental support to this finding: Aβ1-40 aggregation catalyzed by the PAS of AChE might be inhibited by compound 11b in a concentration-dependent manner and seems to occur only with one photochromic form. Computational docking studies provided potential binding modes of the compound. Docking studies and molecular dynamics (MD) simulations for the ring-open and -closed form indicate a difference in binding. Although both forms can interact with the PAS, more stable interactions are observed for the ring-open form based upon stabilization of a water molecule network within the enzyme, whereas the ring-closed form lacks the required conformational flexibility for an analogous binding mode. The photoswitchable inhibitor identified might serve as valuable molecular tool to investigate the different biological properties of AChE as well as its role in pathogenesis of AD in in vitro assays.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.