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Interaction study of two diterpenes, cryptotanshinone and dihydrotanshinone, to human acetylcholinesterase and butyrylcholinesterase by molecular docking and kinetic analysis

Authors :
Wong, Kelvin Kin-Kwan
Ngo, Jacky Chi-Ki
Liu, Sijie
Lin, Huang-quan
Hu, Chun
Shaw, Pang-Chui
Wan, David Chi-Cheong
Wong, Kelvin Kin-Kwan
Ngo, Jacky Chi-Ki
Liu, Sijie
Lin, Huang-quan
Hu, Chun
Shaw, Pang-Chui
Wan, David Chi-Cheong
Publication Year :
2010

Abstract

Alzhemier's disease (AD) is a common form of dementia in the ageing population which is characterized by depositions of amyloids and a cholinergic neurotransmission deficit in the brain. Current therapeutic intervention for AD is primarily based on the inhibition of brain acetylcholinesterase (AChE) to restore the brain acetylcholine level. Cryptotanshinone (CT) and dihydrotanshinone (DT) were diterpenoids extracted from Salvia miltiorrhiza Bge. having anti-cholinesterase activity. Here we characterized the inhibition property of these two diterpenoids towards human AChE and butyrylcholinesterase (BChE). Both CT and DT were found to be mixed non-competitive inhibitors for human AChE and an uncompetitive inhibitor for human BChE. The docking analyses of CT and DT into the active sites of both cholinesterases indicate that they interact with the allosteric site inside the active-site gorge mainly by hydrophobic interactions. © 2010 Elsevier Ireland Ltd.

Details

Database :
OAIster
Notes :
English
Publication Type :
Electronic Resource
Accession number :
edsoai.on1363060543
Document Type :
Electronic Resource