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Evidence-Based Complementary and Alternative Medicine
Volume 2014 (2014), Article ID 524650, 11 pages
http://dx.doi.org/10.1155/2014/524650
Research Article

A Platform for Screening Potential Anticholinesterase Fractions and Components Obtained from Anemarrhena asphodeloides Bge for Treating Alzheimer’s Disease

1School of Traditional Chinese Materia Medica, Shenyang Pharmaceutical University, Shenyang, Liaoning 110016, China
2School of Pharmacy, Shenyang Pharmaceutical University, Shenyang, Liaoning 110016, China
3Key Laboratory of Structure-Based, Drug Design & Discovery, Ministry of Education, Shenyang, Liaoning 110016, China

Received 4 November 2013; Revised 2 March 2014; Accepted 20 March 2014; Published 17 April 2014

Academic Editor: Chuthamanee Suthisisang

Copyright © 2014 Yu Sun et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Alzheimer’s disease (AD) is a neurodegenerative disease characterized by progressive memory loss and cognitive impairment. Cholinesterase inhibitors are widely used for the symptomatic treatment of Alzheimer’s disease to enhance central cholinergic transmission. In this study, a bioactivity-oriented screening platform based on a modified Ellman’s method and HPLC-QTOF MS technique was developed to rapidly screen active agents of Anemarrhena asphodeloides Bge. The 60% ethanol fraction from an ethyl acetate extract exhibited the most potential anticholinesterase activity. Fifteen steroid saponins were identified by the mass spectrum, standards and literature reports. Twenty-five compounds were isolated from the active fraction. The results showed that compounds with the C6–C3–C6 skeleton probably had both AChE and BuChE inhibitory activities. Xanthone and benzene derivatives exhibited no or little activity. Lignans showed weak BuChE inhibitory activity. The steroidal saponins demonstrated moderate or weak AChE inhibitory activity.