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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Acetylcholinesterase / metabolism*
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Anabasine / chemistry
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Anabasine / toxicity*
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Animals
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Caffeine / chemistry
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Caffeine / toxicity*
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Cholinesterase Inhibitors / chemistry
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Cholinesterase Inhibitors / toxicity*
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Electrophorus
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Pyrrolidines / chemistry
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Pyrrolidines / toxicity*
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Structure-Activity Relationship
Substances
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Cholinesterase Inhibitors
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Pyrrolidines
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N-methylpyrrolidine
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Caffeine
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Acetylcholinesterase
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Anabasine