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• W2037847555 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." @default.
• W2037847555 created "2016-06-24" @default.
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• W2037847555 date "2008-05-15" @default.
• W2037847555 modified "2023-10-03" @default.
• W2037847555 title "The cyanobacterial alkaloid nostocarboline: an inhibitor of acetylcholinesterase and trypsin" @default.
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• W2037847555 doi "https://doi.org/10.1007/s10811-008-9335-3" @default.
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