Karadsheh N, Kussie P, Linthicum D S
Department of Veterinary Microbiology and Parasitology, College of Veterinary Medicine, Texas A&M University, College Station 77843-4467.
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.