Structure-activity studies on acetylcholinesterase inhibition in the lycorine series of Amaryllidaceae alkaloids

James McNulty; Jerald J Nair; Jessamyn R L Little; John D Brennan; Jaume Bastida

doi:10.1016/j.bmcl.2010.06.130

Structure-activity studies on acetylcholinesterase inhibition in the lycorine series of Amaryllidaceae alkaloids

Bioorg Med Chem Lett. 2010 Sep 1;20(17):5290-4. doi: 10.1016/j.bmcl.2010.06.130. Epub 2010 Jul 1.

Authors

James McNulty¹, Jerald J Nair, Jessamyn R L Little, John D Brennan, Jaume Bastida

Affiliation

¹ Department of Chemistry and Chemical Biology, McMaster University, Hamilton, Ontario, Canada. jmcnult@mcmaster.ca

PMID: 20655219
DOI: 10.1016/j.bmcl.2010.06.130

Abstract

The synthesis of differentially functionalized analogs of the Amaryllidaceae alkaloid lycorine, accessed via a concise chemoselective silylation strategy, is described uncovering two of the most potent inhibitors of acetylcholinesterase (AChE) identified to date in this series. Important elements of this novel pharmacophore were elucidated through structure-activity relationship (SAR) studies.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Alkaloids / chemistry*
Alkaloids / pharmacology*
Cholinesterase Inhibitors / chemistry*
Cholinesterase Inhibitors / pharmacology*
Structure-Activity Relationship

Substances

Alkaloids
Cholinesterase Inhibitors