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Journal of Applied Phycology

, 21:103 | Cite as

The cyanobacterial alkaloid nostocarboline: an inhibitor of acetylcholinesterase and trypsin

  • Paul G. Becher
  • Heike I. Baumann
  • Karl Gademann
  • Friedrich Jüttner
Article

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 (IC50 = 5.3 µM), 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 (IC50 = 2.8 µM), 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 

Notes

Acknowledgement

This work was supported by the National Science Foundation, Bern, and Hydrobiologie-Limnologie Stiftung, Zürich.

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Copyright information

© Springer Science+Business Media B.V. 2008

Authors and Affiliations

  • Paul G. Becher
    • 1
  • Heike I. Baumann
    • 1
  • Karl Gademann
    • 2
  • Friedrich Jüttner
    • 1
  1. 1.Limnological Station, Institute of Plant BiologyUniversity of ZürichKilchbergSwitzerland
  2. 2.Chemical Synthesis Laboratory, SB-ISIC-LSYNCSwiss Federal Institute of Technology (EPFL)LausanneSwitzerland

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