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Title 

Isolation of cholinesterase and beta-secretase 1 inhibiting compounds from Lycopodiella cernua

Authors 

V T NguyenD C ToM H TranOh Sang HoJ A KimM Y AliM H WooJ S ChoiB S Min

Publisher 

Elsevier

Issue Date 

2015

Citation 

Bioorganic & Medicinal Chemistry, vol. 23, no. 0, pp. 3126-3134

Keywords 

CholinesteraseHydroxy unsaturated fatty acidLycopodiella cernuaSerratene-type triterpenoidsβ-Secretase

Abstract 

Abstract Three new serratene-type triterpenoids (1-3) and a new hydroxy unsaturated fatty acid (13) together with nine known compounds (4-12) were isolated from Lycopodiella cernua. The chemical structures were established using NMR, MS, and Mosher's method. Compound 13 showed the most potent inhibitory activity against acetylcholinesterase (AChE) with an IC50 value of 0.22 μM. For butyrylcholinesterase (BChE) inhibitory activity, 5 showed the most potent activity with an IC50 value of 0.42 μM. Compound 2 showed the most potent activity with an IC50 of 0.23 μM for BACE-1 inhibitory activity. The kinetic activities were investigated to determine the type of enzyme inhibition involved. The types of AChE inhibition shown by compounds 4, 5, and 13 were mixed; BChE inhibition by 5 was competitive, while 2 and 6 showed mixed-types. In addition, molecular docking studies were performed to investigate the interaction of these compounds with the pocket sites of AChE. The docking results revealed that the tested inhibitors 3, 4, and 13 were stably present in several pocket domains of the AChE residue.

ISSN 

0968-0896

Link 

http://dx.doi.org/10.1016/j.bmc.2015.04.080

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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