Dimerization of an inactive fragment of Huperzine A produces a drug with twice the potency of the natural product

Paul R. Carlier, Da Ming Du, Yi Fan Han, Jing Liu, Emanuele Perola, Ian D. Williams, Yuan Ping Pang

Research output: Contribution to journalArticle

82 Scopus citations

Abstract

Simultaneous binding to the catalytic and peripheral sites of acetylcholinesterase (AChE) is invoked to explain why the new drug (S,S)-(-)- 3, in which two aminoquinolinone units are linked by a dodecamethylene tether, is more than twice as potent as the natural product huperzine A (-)-1 in the inhibition of ACHE. In contrast aminoquinolinone (±)-2, which retains much of the functionality of (-)-1, inhibits AChE only very weakly.

Original languageEnglish (US)
Pages (from-to)1775-1777
Number of pages3
JournalAngewandte Chemie - International Edition
Volume39
Issue number10
DOIs
StatePublished - May 15 2000

Keywords

  • Dimerizations
  • Drug research
  • Enzyme inhibitors
  • Natural products
  • Noncovalent interactions

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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