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.
研究了咖啡因、新烟草碱、甲基吡咯烷及其几种衍生物对乙酰胆碱酯酶(AChE)的抑制作用。大多数化合物具有中等抑制活性,半数抑制浓度(IC50)值在87 - 480微摩尔范围内。这些化合物对AChE的抑制作用此前未见报道。这些化合物共有的一个结构特征是吡咯烷环的N - 甲基基团,它可能在与AChE结合中起重要作用。