Oximes: Inhibitors of human recombinant acetylcholinesterase. A structure-activity relationship (SAR) study

Vendula Sepsova, Jana Zdarova Karasova, Jan Korabecny, Rafael Dolezal, Filip Zemek, Brian J. Bennion, Kamil Kuca

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


Acetylcholinesterase (AChE) reactivators were developed for the treatment of organophosphate intoxication. Standard care involves the use of anticonvulsants (e.g., diazepam), parasympatolytics (e.g., atropine) and oximes that restore AChE activity. However, oximes also bind to the active site of AChE, simultaneously acting as reversible inhibitors. The goal of the present study is to determine how oxime structure influences the inhibition of human recombinant AChE (hrAChE). Therefore, 24 structurally different oximes were tested and the results compared to the previous eel AChE (EeAChE) experiments. Structural factors that were tested included the number of pyridinium rings, the length and structural features of the linker, and the number and position of the oxime group on the pyridinium ring.

Original languageEnglish (US)
Pages (from-to)16882-16900
Number of pages19
JournalInternational Journal of Molecular Sciences
Issue number8
StatePublished - 2013
Externally publishedYes


  • Acetylcholinesterase
  • Inhibitors
  • Oximes
  • SAR study

ASJC Scopus subject areas

  • Computer Science Applications
  • Molecular Biology
  • Catalysis
  • Inorganic Chemistry
  • Spectroscopy
  • Organic Chemistry
  • Physical and Theoretical Chemistry


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