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
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.
Access Rights
subscription content
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