Potencies and stereoselectivities of enantiomers of huperzine A for inhibition of rat cortical acetylcholinesterase

Michael McKinney, Jacqueline H. Miller, Fumio Yamada, Werner Tuckmantel, Alan P. Kozikowski

Research output: Contribution to journalArticle

Abstract

The stereoselectivities and mechanisms of the inhibition of rat cortical acetylcholinesterase by the enantiomers of huperzine A were determined. (-)-Huperzine A was the more potent enantiomer with a Ki value of 8 nM. (+)-Huperzine A inhibited the enzyme 38-fold less potently with a Ki value of 300 nM. Racemic huperzine A was about two-fold less potent than the more active isomer, (-)-huperzine A. The mechanism of inhibition of acetylcholinesterase for all three drugs was of the mixed linear competitive type.

Original languageEnglish (US)
Pages (from-to)303-305
Number of pages3
JournalEuropean Journal of Pharmacology
Volume203
Issue number2
DOIs
StatePublished - Oct 15 1991

Keywords

  • (Natural products)
  • Acetylcholine
  • Alzheimer's disease
  • Cerebral cortex
  • Cholinomimetics
  • Stereochemistry

ASJC Scopus subject areas

  • Pharmacology

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