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

Sun Y, Peng Y, Li LG, Zheng LW, Lin DJ, Li LZ, Song SJ - Evid Based Complement Alternat Med (2014)

Bottom Line: The results showed that compounds with the C6-C3-C6 skeleton probably had both AChE and BuChE inhibitory activities.Lignans showed weak BuChE inhibitory activity.The steroidal saponins demonstrated moderate or weak AChE inhibitory activity.

View Article: PubMed Central - PubMed

Affiliation: School of Traditional Chinese Materia Medica, Shenyang Pharmaceutical University, Shenyang, Liaoning 110016, China.

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.

No MeSH data available.


Related in: MedlinePlus

The proposed ESI-MS/MS fragmentation pathway of timosaponin BII.
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Related In: Results  -  Collection


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fig5: The proposed ESI-MS/MS fragmentation pathway of timosaponin BII.

Mentions: Timosaponin BII produced a precursor ion [M + Na]+ at m/z 943.4872 (C45H76O19Na). As the C22 position was an active site, it readily eliminated the 22-hydroxyl residue to produce the thermal degradation ion [M + H – H2O]+ at m/z 903.4982 (C45H75O18), which could generate an ion at m/z 741.4468 [M + H – H2O – 162]+ by further neutral loss of a glucose moiety from the C26 position. At the same time, the product ions at 579.3934 [M + H – H2O – 2×162]+ and 417.3251 [M + H – H2O – 3 × 162]+, which corresponded to skeleton residues by successive losses of terminal hexose, could also be clearly observed. Furthermore, the fragment ion at m/z 273.2139 [417.3251 – C8H16O2]+ was attributed to a skeleton residue by the cleavage of the C20–C22 and C17–C20 bonds due to the presence of a 16,22-epoxy residue and a 22,26-epoxy residue, and then the ion continued to lose H2O to yield an ion at m/z 255.2030 [273.2139 – H2O]+. Major fragmentations proposed for timosaponin BII were presented in Figure 5.


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

Sun Y, Peng Y, Li LG, Zheng LW, Lin DJ, Li LZ, Song SJ - Evid Based Complement Alternat Med (2014)

The proposed ESI-MS/MS fragmentation pathway of timosaponin BII.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4016847&req=5

fig5: The proposed ESI-MS/MS fragmentation pathway of timosaponin BII.
Mentions: Timosaponin BII produced a precursor ion [M + Na]+ at m/z 943.4872 (C45H76O19Na). As the C22 position was an active site, it readily eliminated the 22-hydroxyl residue to produce the thermal degradation ion [M + H – H2O]+ at m/z 903.4982 (C45H75O18), which could generate an ion at m/z 741.4468 [M + H – H2O – 162]+ by further neutral loss of a glucose moiety from the C26 position. At the same time, the product ions at 579.3934 [M + H – H2O – 2×162]+ and 417.3251 [M + H – H2O – 3 × 162]+, which corresponded to skeleton residues by successive losses of terminal hexose, could also be clearly observed. Furthermore, the fragment ion at m/z 273.2139 [417.3251 – C8H16O2]+ was attributed to a skeleton residue by the cleavage of the C20–C22 and C17–C20 bonds due to the presence of a 16,22-epoxy residue and a 22,26-epoxy residue, and then the ion continued to lose H2O to yield an ion at m/z 255.2030 [273.2139 – H2O]+. Major fragmentations proposed for timosaponin BII were presented in Figure 5.

Bottom Line: The results showed that compounds with the C6-C3-C6 skeleton probably had both AChE and BuChE inhibitory activities.Lignans showed weak BuChE inhibitory activity.The steroidal saponins demonstrated moderate or weak AChE inhibitory activity.

View Article: PubMed Central - PubMed

Affiliation: School of Traditional Chinese Materia Medica, Shenyang Pharmaceutical University, Shenyang, Liaoning 110016, China.

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.

No MeSH data available.


Related in: MedlinePlus