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

Abstract

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.