Oligomerization and toxicity of Aß fusion proteins

Oligomerization and toxicity of Aß fusion proteins

This study has found that the Maltose binding protein Aß42 fusion protein (MBP-Aß42) forms soluble oligomers while the shorter MBP-Aß16 fusion and control MBP did not. MBP-Aß42, but neither MBP-Aß16 nor control MBP, was toxic in a dose-dependent manner in both yeast and primary cortical neuronal cel...

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Bibliographic Details
Main Authors: Caine, J., Bharadwaj, Prashant, Sankovich, S., Ciccotosto, G., Streltsov, V., Varghese, J.
Format: Journal Article
Published: 2011
Online Access:http://hdl.handle.net/20.500.11937/5565
Description
Summary:This study has found that the Maltose binding protein Aß42 fusion protein (MBP-Aß42) forms soluble oligomers while the shorter MBP-Aß16 fusion and control MBP did not. MBP-Aß42, but neither MBP-Aß16 nor control MBP, was toxic in a dose-dependent manner in both yeast and primary cortical neuronal cells. This study demonstrates the potential utility of MBP-Aß42 as a reagent for drug screening assays in yeast and neuronal cell cultures and as a candidate for further Aß42 characterization. © 2011 .

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