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Determining acetylcholinesterase inhibitory activity in plant extracts using a fluorimetric flow assay
In Kyung Rhee1, Natalie Appels, Teus Luijendijk
1Division of Pharmacognosy, Leiden/Amsterdam Centre for Drug Research, Gorlaeus Laboratories, Leiden University, PO Box 9502, 2300 RA Leiden, The Netherlands.
Abstract:
A fluorometric assay for acetylcholinesterase inhibitory activity was developed in a flow system using the fluorogenic substrate 7-acetoxy-1-methyl quinolinium iodide which is hydrolysed to the highly fluorescent 7-hydroxy-1-methyl quinolinium iodide. The detection limit of galanthamine is 0.5 microM, which is about 20 times more sensitive than in the colorimetric flow assay. In the presence of 30% methanol or of 5% acetonitrile, about 70% of the enzyme activity could still be detected. Various plant extracts have been screened using the described system including bulbs of Galanthus nivalis, Eucharis amazonica (E. x grandiflora), Crinum powelli and Nerine bowdenii (all members of the Amaryllidaceae), which showed strong AchE inhibitory activity.