Cargando…

Primary Investigation for the Mechanism of Biatractylolide from Atractylodis Macrocephalae Rhizoma as an Acetylcholinesterase Inhibitor

Biatractylolide was isolated from ethyl acetate extract of dried Atractylodis Macrocephalae Rhizoma root by multistep chromatographic processing. Structure of biatractylolide was confirmed by (1)H-NMR and (13)C-NMR. The IC(50) on acetylcholinesterase (AChE) activity was 6.5458 μg/mL when the control...

Descripción completa

Detalles Bibliográficos
Autores principales: Xie, Yong-Chao, Ning, Ning, Zhu, Li, Li, Dan-Ning, Feng, Xing, Yang, Xiao-Ping
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5013199/
https://www.ncbi.nlm.nih.gov/pubmed/27642355
http://dx.doi.org/10.1155/2016/7481323
_version_ 1782452116657274880
author Xie, Yong-Chao
Ning, Ning
Zhu, Li
Li, Dan-Ning
Feng, Xing
Yang, Xiao-Ping
author_facet Xie, Yong-Chao
Ning, Ning
Zhu, Li
Li, Dan-Ning
Feng, Xing
Yang, Xiao-Ping
author_sort Xie, Yong-Chao
collection PubMed
description Biatractylolide was isolated from ethyl acetate extract of dried Atractylodis Macrocephalae Rhizoma root by multistep chromatographic processing. Structure of biatractylolide was confirmed by (1)H-NMR and (13)C-NMR. The IC(50) on acetylcholinesterase (AChE) activity was 6.5458 μg/mL when the control IC(50) value of huperzine A was 0.0192 μg/mL. Molecular Docking Software (MOE) was used to discover molecular sites of action between biatractylolide and AChE protein by regular molecular docking approaches. Moreover, biatractylolide downregulated the expression of AChE of MEF and 293T cells in a dose-dependent manner. These results demonstrated that the molecular mechanisms of inhibitory activities of biatractylolide on AChE are not only through binding to AChE, but also via reducing AChE expression by inhibiting the activity of GSK3β.
format Online
Article
Text
id pubmed-5013199
institution National Center for Biotechnology Information
language English
publishDate 2016
publisher Hindawi Publishing Corporation
record_format MEDLINE/PubMed
spelling pubmed-50131992016-09-18 Primary Investigation for the Mechanism of Biatractylolide from Atractylodis Macrocephalae Rhizoma as an Acetylcholinesterase Inhibitor Xie, Yong-Chao Ning, Ning Zhu, Li Li, Dan-Ning Feng, Xing Yang, Xiao-Ping Evid Based Complement Alternat Med Research Article Biatractylolide was isolated from ethyl acetate extract of dried Atractylodis Macrocephalae Rhizoma root by multistep chromatographic processing. Structure of biatractylolide was confirmed by (1)H-NMR and (13)C-NMR. The IC(50) on acetylcholinesterase (AChE) activity was 6.5458 μg/mL when the control IC(50) value of huperzine A was 0.0192 μg/mL. Molecular Docking Software (MOE) was used to discover molecular sites of action between biatractylolide and AChE protein by regular molecular docking approaches. Moreover, biatractylolide downregulated the expression of AChE of MEF and 293T cells in a dose-dependent manner. These results demonstrated that the molecular mechanisms of inhibitory activities of biatractylolide on AChE are not only through binding to AChE, but also via reducing AChE expression by inhibiting the activity of GSK3β. Hindawi Publishing Corporation 2016 2016-08-24 /pmc/articles/PMC5013199/ /pubmed/27642355 http://dx.doi.org/10.1155/2016/7481323 Text en Copyright © 2016 Yong-Chao Xie et al. https://creativecommons.org/licenses/by/4.0/ 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.
spellingShingle Research Article
Xie, Yong-Chao
Ning, Ning
Zhu, Li
Li, Dan-Ning
Feng, Xing
Yang, Xiao-Ping
Primary Investigation for the Mechanism of Biatractylolide from Atractylodis Macrocephalae Rhizoma as an Acetylcholinesterase Inhibitor
title Primary Investigation for the Mechanism of Biatractylolide from Atractylodis Macrocephalae Rhizoma as an Acetylcholinesterase Inhibitor
title_full Primary Investigation for the Mechanism of Biatractylolide from Atractylodis Macrocephalae Rhizoma as an Acetylcholinesterase Inhibitor
title_fullStr Primary Investigation for the Mechanism of Biatractylolide from Atractylodis Macrocephalae Rhizoma as an Acetylcholinesterase Inhibitor
title_full_unstemmed Primary Investigation for the Mechanism of Biatractylolide from Atractylodis Macrocephalae Rhizoma as an Acetylcholinesterase Inhibitor
title_short Primary Investigation for the Mechanism of Biatractylolide from Atractylodis Macrocephalae Rhizoma as an Acetylcholinesterase Inhibitor
title_sort primary investigation for the mechanism of biatractylolide from atractylodis macrocephalae rhizoma as an acetylcholinesterase inhibitor
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5013199/
https://www.ncbi.nlm.nih.gov/pubmed/27642355
http://dx.doi.org/10.1155/2016/7481323
work_keys_str_mv AT xieyongchao primaryinvestigationforthemechanismofbiatractylolidefromatractylodismacrocephalaerhizomaasanacetylcholinesteraseinhibitor
AT ningning primaryinvestigationforthemechanismofbiatractylolidefromatractylodismacrocephalaerhizomaasanacetylcholinesteraseinhibitor
AT zhuli primaryinvestigationforthemechanismofbiatractylolidefromatractylodismacrocephalaerhizomaasanacetylcholinesteraseinhibitor
AT lidanning primaryinvestigationforthemechanismofbiatractylolidefromatractylodismacrocephalaerhizomaasanacetylcholinesteraseinhibitor
AT fengxing primaryinvestigationforthemechanismofbiatractylolidefromatractylodismacrocephalaerhizomaasanacetylcholinesteraseinhibitor
AT yangxiaoping primaryinvestigationforthemechanismofbiatractylolidefromatractylodismacrocephalaerhizomaasanacetylcholinesteraseinhibitor