Becher, Paul
- University of Zürich
Abstract
Preselected cyanobacterial strains (available from culture collections and our own isolates), belonging primarily to the heterocystous cluster, were screened for inhibitors against butyrylcholinesterase. About one-half of the extracts exhibited inhibitory activity. Nostocarboline, the responsible metabolite in Nostoc 78-12A, was studied in more detail as an acetylcholinesterase (AChE) inhibitor. The compound showed potent activity against this enzyme (IC(50) = 5.3 A mu M), and the Michaelis-Menten kinetics indicated a non-competitive component in the inhibitory mechanism. In addition, nostocarboline turned out to be a potent inhibitor of trypsin (IC(50) = 2.8 A mu M), and thus is the first described cyanobacterial serine protease inhibitor of an alkaloid structure. The function of nostocarboline in aquatic ecosystems and its potential as a lead compound for the development of useful therapeutic AChE inhibitors is discussed.
Keywords
Screening; Cyanobacteria; Nostoc; Serine protease; Alzheimer's disease
Published in
Journal of Applied Phycology
2009, volume: 21, number: 1, pages: 103-110
Publisher: SPRINGER
SLU Authors
UKÄ Subject classification
Ecology
Publication identifier
- DOI: https://doi.org/10.1007/s10811-008-9335-3
Permanent link to this page (URI)
https://res.slu.se/id/publ/42845