Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.cbi.2010.03.042
Title: Anti-amyloidogenic effect of AA3E2 attenuates β-amyloid induced toxicity in SK-N-MC cells
Authors: Shaykhalishahi, H.
Taghizadeh, M.
Yazdanparast, R.
Chang, Y.-T. 
Keywords: Aβ1-42 fibril
AA3E2
Alzheimer's disease
Anti-amyloidogenic
Docking
Issue Date: Jun-2010
Citation: Shaykhalishahi, H., Taghizadeh, M., Yazdanparast, R., Chang, Y.-T. (2010-06). Anti-amyloidogenic effect of AA3E2 attenuates β-amyloid induced toxicity in SK-N-MC cells. Chemico-Biological Interactions 186 (1) : 16-23. ScholarBank@NUS Repository. https://doi.org/10.1016/j.cbi.2010.03.042
Abstract: β-Amyloid peptide (Aβ) is believed to play a recognized role in pathogenesis of Alzheimer's disease (AD). Self-association of Aβ peptide into amyloid fibrils causes neurotoxicity. Compounds capable of interfering with Aβ-Aβ interaction through binding to nucleation sites can inhibit Aβ amyloidogenesis and Aβ-induced cytotoxicity. AA3E2 is a triazine-derivative whose anti-amyloidogenic ability has previously been established. In the present study, we evaluated the protective effect of AA3E3 against Aβ1-42-induced toxicity in SK-N-MC cell line. The cell exposure to the co-incubated Aβ1-42 with AA3E2 decreased the cell viability loss dose-dependently, compared to cells exposed to Aβ1-42 fibrils.Co-incubation with AA3E2 also attenuated the ROS production, activation of caspase-3 and the extent of apoptotic cell death induced by Aβ1-42 fibril. Moreover, the 3D structure of the molecular associates between Aβ1-42 and AA3E2 were theoretically determined by docking studies. Our docking data indicated that AA3E2 inhibits the formation of Aβ fibril likely via binding to the nucleation site within the hydrophobic region of Aβ (KLVFF). These observations provide the background for future design of more elegant β-breaking agents for dissolution of Aβ fibrillar aggregates. © 2010 Elsevier Ireland Ltd.
Source Title: Chemico-Biological Interactions
URI: http://scholarbank.nus.edu.sg/handle/10635/93114
ISSN: 00092797
DOI: 10.1016/j.cbi.2010.03.042
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