title: 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.
authors.affiliation: Department of Veterinary Microbiology and Parasitology, College of Veterinary Medicine, Texas A&M University, College Station 77843-4467.
authors.forename: N
authors.initials: N
authors.lastname: Karadsheh
authors.forename: P
authors.initials: P
authors.lastname: Kussie
authors.forename: D S
authors.initials: DS
authors.lastname: Linthicum
mesh_terms: D000110:Acetylcholinesterase / Q000378:metabolism*; D000691:Anabasine / Q000737:chemistry / Q000633:toxicity*; D000818:Animals; D002110:Caffeine / Q000737:chemistry / Q000633:toxicity*; D002800:Cholinesterase Inhibitors / Q000737:chemistry / Q000633:toxicity*; D004593:Electrophorus; D011759:Pyrrolidines / Q000737:chemistry / Q000633:toxicity*; D013329:Structure-Activity Relationship
chemical_list: D002800:Cholinesterase Inhibitors; D011759:Pyrrolidines; C054965:N-methylpyrrolidine; D002110:Caffeine; D000110:Acetylcholinesterase; D000691:Anabasine