Planta Med 2016; 82(S 01): S1-S381
DOI: 10.1055/s-0036-1596486
Abstracts
Georg Thieme Verlag KG Stuttgart · New York

Chemical constituents from Agrimonia pilosa with their protein tyrosine phosphatase and acetylcholinesterase inhibitory activities

DH Nguyen
1   College of Pharmacy, Catholic University of Daegu, Gyeongsan 38430, Republic of Korea
2   Phutho College of Pharmacy, Viettri City, Phutho Province 290000, Vietnam
,
DD Le
1   College of Pharmacy, Catholic University of Daegu, Gyeongsan 38430, Republic of Korea
,
UM Seo
1   College of Pharmacy, Catholic University of Daegu, Gyeongsan 38430, Republic of Korea
,
TT Nguyen
1   College of Pharmacy, Catholic University of Daegu, Gyeongsan 38430, Republic of Korea
,
JS Choi
3   Department of Food Science & Nutrition, Pukyong National University, Busan 608 – 737, Republic of Korea
,
MH Woo
1   College of Pharmacy, Catholic University of Daegu, Gyeongsan 38430, Republic of Korea
› Author Affiliations
Further Information

Publication History

Publication Date:
14 December 2016 (online)

 

Agrimonia pilosa Ledeb., a perennial herb, belongs to the Rosaceae family. The whole plant A. pilosa has been used traditionally as hemostatic, antimalarial, and antidysenteric in Chinese herbal medicine for a long time [1,2]. Two new flavanonol glucoside isomers, (2S,3R) dihydrokaempferol 3-O-β-<scaps>D</scaps>-glucoside (1) and (2R,3S) dihydrokaempferol 3-O-β-<scaps>D</scaps>-glucoside (2), were isolated from the aerial parts of A. pilosa, along with 12 known compounds (3-14). Their structures were determined on the basis of spectroscopic analyses. In addition, all the isolates were evaluated for PTP1B inhibitory activity. Among them, compounds 13 and 14 displayed potential inhibitory activity against PTP1B with IC50 values of 7.14 ± 1.75 and 7.73 ± 0.24µM, respectively. Furthermore, all the isolated compounds were found to inhibit AChE with IC50 values ranging from 62.96 ± 0.35 to 118.32 ± 0.09µM.

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Keywords: Agrimonia pilosa, Flavanonol glucosides, Protein tyrosine phosphatase 1B, acetylcholinesterase.

References:

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