Synthesis, in vitro acetylcholinesterase inhibitory activity and molecular docking of new acridine-coumarin hybrids
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články
PubMed
28601645
DOI
10.1016/j.ijbiomac.2017.06.006
PII: S0141-8130(16)32819-7
Knihovny.cz E-zdroje
- Klíčová slova
- Acridine, Alzheimeŕs disease, Cholinesterase, Cholinesterase inhibitors, Coumarin, Tacrine,
- MeSH
- acetylcholinesterasa chemie metabolismus MeSH
- akridiny chemická syntéza chemie metabolismus farmakologie MeSH
- cholinesterasové inhibitory chemická syntéza chemie metabolismus farmakologie MeSH
- inhibiční koncentrace 50 MeSH
- katalytická doména MeSH
- kumariny chemie MeSH
- lidé MeSH
- simulace molekulového dockingu * MeSH
- techniky syntetické chemie MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- acetylcholinesterasa MeSH
- akridiny MeSH
- cholinesterasové inhibitory MeSH
- coumarin MeSH Prohlížeč
- kumariny 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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