8-Hydroxydihydrochelerythrine and 8-Hydroxydihydrosanguinarine with a Potent Acetylcholinesterase Inhibitory Activity from Chelidonium majus L

• Published in: Biological & pharmaceutical bulletin Vol. 29; no. 11; pp. 2317 - 2320
• Main Authors: Cho, Kyung-Mi, Yoo, Ick-Dong, Kim, Won-Gon
• Format: Journal Article
• Language: English
• Published: Japan The Pharmaceutical Society of Japan 01.11.2006; Japan Science and Technology Agency
• Subjects: 8-hydroxydihydrochelerythrine; 8-hydroxydihydrosanguinarine; acetylcholinesterase; Acetylcholinesterase - metabolism; Berberine - chemistry; Berberine - isolation & purification; Berberine - pharmacology; Butyrylcholinesterase - metabolism; Chelidonium - chemistry; Chelidonium majus L; Chloroform - chemistry; Cholinesterase Inhibitors - chemistry; Cholinesterase Inhibitors - isolation & purification; Cholinesterase Inhibitors - pharmacology; Chromatography - methods; Dose-Response Relationship, Drug; Ethanol - chemistry; Herbal Medicine; Heterocyclic Compounds, 4 or More Rings - chemistry; Heterocyclic Compounds, 4 or More Rings - isolation & purification; Heterocyclic Compounds, 4 or More Rings - pharmacology; Methanol - chemistry; Molecular Structure; Nuclear Magnetic Resonance, Biomolecular - methods; Plant Components, Aerial - chemistry; Plant Extracts - chemistry; Plant Extracts - isolation & purification; Plant Extracts - pharmacology; Polycyclic Compounds - chemistry; Polycyclic Compounds - isolation & purification; Polycyclic Compounds - pharmacology
• ISSN: 0918-6158; 1347-5215
• DOI: 10.1248/bpb.29.2317

Ethanol extract of the aerial portion of Chelidonium majus L. inhibited acetylcholinesterase (AChE) activity without a significant inhibition of butyrylcholinesterase (BuChE). Using mass spectrometry and NMR studies, three active constituents were isolated and identified: 8-hydroxydihydrochelerythrine (1), 8-hydroxydihydrosanguinarine (2), and berberine (3). Compounds 1—3 showed potent inhibitory activity against AChE, with IC50 (μM) values of 0.61—1.85. Compound 1 exhibited competitive and selective inhibition for AChE.