Acetylcholinesterase inhibition by products generated in situ from the transformation of N-arylisomaleimides

Juan A. Guevara, José G. Trujillo, Delia Quintana, Hugo A. Jiménez, Mónica G. Arellano, José R. Bahena, Feliciano Tamay, Fabiola J. Ciprés

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4 Scopus citations

Abstract

When N-arylisomaleimides were transformed under enzymatic reaction conditions, the transformation reaction proved to be influenced by electronic effects. This was demonstrated qualitatively by 1H NMR spectroscopy and quantitatively by monitoring the kinetic of isomerization of N-phenylisomaleimide to N-phenylmaleimide. Subsequently, the first pseudo-order and activation energy (Ea) of the process were determined. The compounds showed in situ influence on AChE inhibition. The derivatives with electron-withdrawing groups exhibited a better effect than those having electron-donating groups. The in silico experiments show that the ligands evaluated established interactions with the CAS site. This suggests that these compounds could be useful for generating better reversible and competitive inhibitors of AChE.

Original languageEnglish
Pages (from-to)989-1003
Number of pages15
JournalMedicinal Chemistry Research
Volume27
Issue number3
DOIs
StatePublished - 1 Mar 2018

Keywords

  • Acetylcholinesterase inhibitors
  • Alzheimer’s disease
  • Catalysis
  • Isomerization kinetics
  • N-arylimides
  • N-arylisomaleimides

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