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[PMID]: | 28708094 | [Au] Autor: | Siatka T; Adamcová M; Opletal L; Cahlíková L; Jun D; Hrabinová M; Kunes J; Chlebek J |
[Ad] Address: | Department of Pharmacognosy, Faculty of Pharmacy, Charles University, Akademika Heyrovského 1203, 500 05 Hradec Králové, Czech Republic. tomas.siatka@faf.cuni.cz. | [Ti] Title: | Cholinesterase and Prolyl Oligopeptidase Inhibitory Activities of Alkaloids from Argemone platyceras (Papaveraceae). | [So] Source: | Molecules;22(7), 2017 Jul 14. | [Is] ISSN: | 1420-3049 | [Cp] Country of publication: | Switzerland | [La] Language: | eng | [Ab] Abstract: | Alzheimer's disease is an age-related, neurodegenerative disorder, characterized by cognitive impairment and restrictions in activities of daily living. This disease is the most common form of dementia with complex multifactorial pathological mechanisms. Many therapeutic approaches have been proposed. Among them, inhibition of acetylcholinesterase, butyrylcholinesterase, and prolyl oligopeptidase can be beneficial targets in the treatment of Alzheimer's disease. Roots, along with aerial parts of , were extracted with ethanol and fractionated on an alumina column using light petrol, chloroform and ethanol. Subsequently, repeated preparative thin-layer chromatography led to the isolation of (+)-laudanosine, protopine, (-)-argemonine, allocryptopine, (-)-platycerine, (-)-munitagine, and (-)-norargemonine belonging to pavine, protopine and benzyltetrahydroisoquinoline structural types. Chemical structures of the isolated alkaloids were elucidated by optical rotation, spectroscopic and spectrometric analysis (NMR, MS), and comparison with literature data. (+)-Laudanosine was isolated from for the first time. Isolated compounds were tested for human blood acetylcholinesterase, human plasma butyrylcholinesterase and recombinant prolyl oligopeptidase inhibitory activity. The alkaloids inhibited the enzymes in a dose-dependent manner. The most active compound (-)-munitagine, a pavine alkaloid, inhibited both acetylcholinesterase and prolyl oligopeptidase with IC values of 62.3 ± 5.8 µM and 277.0 ± 31.3 µM, respectively. | [Pt] Publication type: | JOURNAL ARTICLE | [Em] Entry month: | 1707 | [Cu] Class update date: |
170714 | [Lr] Last revision date: | 170714 | [St] Status: | In-Process |
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