Back to Search
Start Over
Oligomerization and toxicity of Aβ fusion proteins.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2011 Jun 10; Vol. 409 (3), pp. 477-82. Date of Electronic Publication: 2011 May 12. - Publication Year :
- 2011
-
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.<br /> (Crown Copyright © 2011. Published by Elsevier Inc. All rights reserved.)
- Subjects :
- Amyloid beta-Peptides genetics
Animals
Apoptosis
Cerebral Cortex cytology
Maltose-Binding Proteins chemistry
Maltose-Binding Proteins genetics
Maltose-Binding Proteins toxicity
Mice
Peptide Fragments genetics
Protein Multimerization
Recombinant Fusion Proteins genetics
Saccharomyces cerevisiae drug effects
Solubility
Amyloid beta-Peptides chemistry
Amyloid beta-Peptides toxicity
Neurons drug effects
Peptide Fragments chemistry
Peptide Fragments toxicity
Recombinant Fusion Proteins chemistry
Recombinant Fusion Proteins toxicity
Subjects
Details
- Language :
- English
- ISSN :
- 1090-2104
- Volume :
- 409
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 21600886
- Full Text :
- https://doi.org/10.1016/j.bbrc.2011.05.029