Oligomerization and Toxicity of Aβ Fusion Proteins

Document Type

Journal Article

Keywords

Amyloid beta peptide, Alzheimer's disease, MBP fusion, Toxicity

Publisher

Academic Press

Faculty

Faculty of Computing, Health and Science

School

School of Medical Sciences / Centre of Excellence for Alzheimer's Disease Research and Care

RAS ID

12475

Comments

Caine, J., Bharadwaj, P. , Sankovich, S., Ciccotosto, G., Streltsov, V., & Varghese, J. (2011). Oligomerization and toxicity of Aβ fusion proteins. Biochemical and Biophysical Research Communications, 409(3), 477-482. Available here

Abstract

This study has found that the Maltose binding protein Aβ42 fusion protein (MBP-Aβ42 ) forms soluble oligomers while the shorter MBP-Aβ16 fusion and control MBP did not. MBP-Aβ42. but neither MBP-Aβ16 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-Aβ42 as a reagent for drug screening assays in yeast and neuronal cell cultures and as a candidate for further Aβ42 characterization.

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Link to publisher version (DOI)

10.1016/j.bbrc.2011.05.029