Synthesis, in vitro acetylcholinesterase inhibitory activity and molecular docking of new acridine-coumarin hybrids
Language English Country Netherlands Media print-electronic
Document type Journal Article
PubMed
28601645
DOI
10.1016/j.ijbiomac.2017.06.006
PII: S0141-8130(16)32819-7
Knihovny.cz E-resources
- Keywords
- Acridine, Alzheimeŕs disease, Cholinesterase, Cholinesterase inhibitors, Coumarin, Tacrine,
- MeSH
- Acetylcholinesterase chemistry metabolism MeSH
- Acridines chemical synthesis chemistry metabolism pharmacology MeSH
- Cholinesterase Inhibitors chemical synthesis chemistry metabolism pharmacology MeSH
- Inhibitory Concentration 50 MeSH
- Catalytic Domain MeSH
- Coumarins chemistry MeSH
- Humans MeSH
- Molecular Docking Simulation * MeSH
- Chemistry Techniques, Synthetic MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Acetylcholinesterase MeSH
- Acridines MeSH
- Cholinesterase Inhibitors MeSH
- coumarin MeSH Browser
- Coumarins MeSH
A novel series of acridine-coumarin hybrids was synthesized and biologically evaluated for their potential inhibitory effect on both acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE). The newly synthesized derivatives 9a-d have shown higher activity against human AChE (hAChE) compared with 7-MEOTA as the standard drug. Among them derivative 9b exhibited the most potent acetylcholinesterase inhibitory activity, with an IC50 value of 5.85μM compared with 7-MEOTA (IC50=15μM). Molecular modelling studies were performed to predict the binding modes of compounds 9b, 9c and 9f with hAChE/hBuChE.
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