Racemic N1-norphenserine and its enantiomers: Unpredicted inhibition of human acetyl- and butyrylcholinesterase and β-amyloid precursor protein in vitro

Qian Sheng Yu, Weiming Luo, Harold W. Holloway, Tada Utsuki, Tracy Ann Perry, Debomoy K. Lahiri, Nigel H. Greig, Arnold Brossi

Research output: Contribution to journalArticle

18 Scopus citations

Abstract

The optically pure enantiomers of N1-norphenserine (15, 16) were synthesized and its racemate 17 was prepared by mixing equal parts of each enantiomer. (-)-N1-Norphenserine (15) was prepared by partial synthesis initiated from the natural product, (-)-physostigmine (1). (+)-N 1-Norphenserine (16) was prepared by total synthesis using the Julian oxindole route, with modifications. The in vitro inhibitory activities of 15-17 were quantified against human erythrocyte AChE and plasma BChE as well as against human neuroblastoma cell β-amyloid precursor protein secretion in cell culture. All were active. Racemic compound (17) with a high AChE and β-amyloid precursor protein inhibitory action may warrant further assessment in Alzheimer's disease models.

Original languageEnglish (US)
Pages (from-to)529-539
Number of pages11
JournalHeterocycles
Volume61
StatePublished - Dec 31 2003

ASJC Scopus subject areas

  • Analytical Chemistry
  • Pharmacology
  • Organic Chemistry

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