Panaxindole, a novel indole alkaloid N-glucoside from the leaves of Panax vietnamensis Ha et Grushv. (Vietnamese ginseng)

Vietnamese ginseng ( Panax vietnamensis Ha and Grushv., Araliaceae) is indigenous in the central highlands of Vietnam and the southernmost distribution in the Panax genus. Like other ginseng, Vietnamese ginseng is well known has been used as a tonic and for management of certain diseases in the trad...

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Veröffentlicht in:Journal of natural medicines 2023-09, Vol.77 (4), p.972-977
Hauptverfasser: Vu, Van-Tuan, Nguyen, Ngoc-Hieu, Anh, Nguyen Thi Hoang, Tung, Pham Ha Thanh, Thuong, Phuong Thien, Tung, Nguyen-Huu
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Sprache:eng
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Zusammenfassung:Vietnamese ginseng ( Panax vietnamensis Ha and Grushv., Araliaceae) is indigenous in the central highlands of Vietnam and the southernmost distribution in the Panax genus. Like other ginseng, Vietnamese ginseng is well known has been used as a tonic and for management of certain diseases in the traditional medicine. Nevertheless, it is noteworthy that in respect to the long history in use and systematic studied on Korean ginseng ( P. ginseng ), American ginseng ( P. quinquefolius ), Japanese ginseng ( P. japonicus ), and Chinese ginseng ( P. notoginseng ), the up-to-date published database on Vietnamese ginseng is relatively much less extensive. In our ongoing research on the promising Vietnamese medicinal plants, the present phytochemical investigation of the ethanol extract of the leaves of Panax vietnamensis led to the isolation of three compounds ( 1 – 3 ), including a new indole alkaloid N -glycoside ( 1 ) and two known compounds. Their structures were elucidated based on extensive physiochemical and chemical methods, especially the interpretation of NMR and MS spectra. The absolute configuration of 1 was determined based on the comparison of its experimental and theoretical ECD spectra along with NMR calculation. Compound 1 is naturally isolated N -glycoside, which is rarely found in natural products. The isolated compounds showed weak or no inhibitory activity against acetylcholinesterase enzyme (AChE). Graphical abstract
ISSN:1340-3443
1861-0293
DOI:10.1007/s11418-023-01728-4