Inhibition of acetylcholinesterase by caffeine, anabasine, methyl pyrrolidine and their derivatives

Toxicol Lett. 1991 Mar;55(3):335-42. doi: 10.1016/0378-4274(91)90015-x.


The inhibition of acetylcholinesterase (AChE) by caffeine, anabasine, methylpyrrolidine and several derivatives was examined. Most of the compounds had moderate inhibitory activity with I50 values in the range of 87-480 microM. The inhibition of AChE by these compounds has not been previously reported. A structural feature common to these compounds is the N-methyl determinant of the pyrrolidine ring which may be important in binding to the AChE.

Publication types

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

MeSH terms

  • Acetylcholinesterase / metabolism*
  • Anabasine / chemistry
  • Anabasine / toxicity*
  • Animals
  • Caffeine / chemistry
  • Caffeine / toxicity*
  • Cholinesterase Inhibitors / chemistry
  • Cholinesterase Inhibitors / toxicity*
  • Electrophorus
  • Pyrrolidines / chemistry
  • Pyrrolidines / toxicity*
  • Structure-Activity Relationship


  • Cholinesterase Inhibitors
  • Pyrrolidines
  • N-methylpyrrolidine
  • Caffeine
  • Acetylcholinesterase
  • Anabasine