Structural insights to investigate Conypododiol as a dual cholinesterase inhibitor from Asparagus adscendens

Khan, Inamullah, Nisar, Muhammad, Khan, Nematullah, Saeed, Muhammad, Nadeem, Said, Fazal-ur-Rehman, Ali, Farooq, Karim, Nasiara, Kaleem, Waqar Ahmad, Qayum, Mughal, Ahmad, Hanif and Khan, Ihsan Ali (2010) Structural insights to investigate Conypododiol as a dual cholinesterase inhibitor from Asparagus adscendens. Fitoterapia, 81 8: 1020-1025. doi:10.1016/j.fitote.2010.06.022


Author Khan, Inamullah
Nisar, Muhammad
Khan, Nematullah
Saeed, Muhammad
Nadeem, Said
Fazal-ur-Rehman
Ali, Farooq
Karim, Nasiara
Kaleem, Waqar Ahmad
Qayum, Mughal
Ahmad, Hanif
Khan, Ihsan Ali
Title Structural insights to investigate Conypododiol as a dual cholinesterase inhibitor from Asparagus adscendens
Formatted title
Structural insights to investigate Conypododiol as a dual cholinesterase inhibitor from Asparagus adscendens
Journal name Fitoterapia   Check publisher's open access policy
ISSN 0367-326X
Publication date 2010-12-01
Sub-type Article (original research)
DOI 10.1016/j.fitote.2010.06.022
Open Access Status Not yet assessed
Volume 81
Issue 8
Start page 1020
End page 1025
Total pages 6
Place of publication Amsterdam, Netherlands
Publisher Elsevier BV
Language eng
Formatted abstract
The main aim of the current study was to explore molecular insights for potentially new dual cholinesterase inhibitor(s) from Asparagus adscendens via molecular docking. This medicinal plant is traditionally used as a nerve tonic and remedy for memory impairments. Conypododiol was isolated from the chloroform fraction of methanolic extract of A. adscendens, based on bioactivity guided isolation. Conypododiol exhibited significant inhibition of both acetylcholinesterase and butyrylcholinesterase, having the IC50 values 2.17 ± 0.1 μM and 11.21 ± 0.1 μM, respectively. IC50 values of the standard compound Galanthamine for both the enzymes were 0.537 ± 0.018 μM and 8.6 ± 0.27 μM, respectively. Based on MTT cytotoxicity assay, Conypododiol was found safe against LCMK-2 monkey kidney epithelial cells and mice hepatocytes. Molecular docking studies revealed the hydrogen bonding interactions of Conypododiol with His440 and Ser200 at esteratic site (ES), and also with Tyr334 at peripheral anionic site (PAS) of the aromatic gorge of acetylcholinesterase. Simultaneous contacts of Conypododiol with PAS and ES shows its significance as a bivalent ligand. This preliminary study highlighted the potential of Conypododiol to be further developed and modified as new lead compound identified by its folk use.
Keyword Acetylcholineterase
Asparagus adscendens
Butyrylcholinesterase
Conypododiol
Molecular docking
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: UQ Centre for Clinical Research Publications
 
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