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 language | English |
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Pages (from-to) | 1775-1777 |
Number of pages | 3 |
Journal | Angewandte Chemie - International Edition |
Volume | 39 |
Issue number | 10 |
DOIs | |
Publication status | Published - 15 May 2000 |
Externally published | Yes |
Keywords
- Dimerizations
- Drug research
- Enzyme inhibitors
- Natural products
- Noncovalent interactions
ASJC Scopus subject areas
- Catalysis
- General Chemistry