Design and synthesis of novel coumarin-pyridinium hybrids: in vitro cholinesterase inhibitory activity

Fahimeh Vafadarnejad, Mohammad Mahdavi, Elahe Karimpour-Razkenari, Najmeh Edraki, Bilqees Sameem, Mahnaz Khanavi, Mina Saeedi, Tahmineh Akbarzadeh*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

39 Citations (Scopus)

Abstract

A novel series of coumarin-pyridinium hybrids were synthesized and evaluated as inhibitors of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) using Ellman's method. Among synthesized compounds, 1-(3-fluorobenzyl)-4-((2-oxo-2H-chromene-3-carboxamido)methyl)pyridinium bromide (7l) was found to be the most active compound toward AChE (IC50 = 10.14 µM), 1-(3-chlorobenzyl)-3-((2-oxo-2H-chromene-3-carboxamido)methyl)pyridinium bromide (7g) and 1-(2,3-dichlorobenzyl)-3-((2-oxo-2H-chromene-3-carboxamido)methyl)pyridinium chloride (7h) depicted the best BChE inhibitory activity (IC50s = 0.32 and 0.43 µM, respectively). Although most compounds showed moderate to good anti-AChE activity, their anti-BChE activity was more significant and compound 7g was found as the most selective BChE with SI of 101.18. Also, kinetic study of the compounds 7g and 7l displayed a mixed type inhibition for both AChE and BChE. Furthermore, they were evaluated against β-secretase; however, they showed low inhibitory activity.

Original languageEnglish
Pages (from-to)311-319
Number of pages9
JournalBioorganic Chemistry
Volume77
DOIs
Publication statusPublished - Apr 2018
Externally publishedYes

Keywords

  • Cholinesterases
  • Coumarins
  • Docking study
  • Kinetic study
  • Pyridinium salts
  • β-secretase (BACE1)

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