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

Int J Mol Sci. 2013 Aug 16;14(8):16882-900. doi: 10.3390/ijms140816882.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Acetylcholinesterase / chemistry*
  • Catalytic Domain
  • Cholinesterase Inhibitors / chemistry*
  • Humans
  • Hydrogen Bonding
  • Molecular Docking Simulation
  • Oximes / chemistry*
  • Protein Binding
  • Structure-Activity Relationship


  • Cholinesterase Inhibitors
  • Oximes
  • Acetylcholinesterase