Oligomerization and toxicity of Aβ fusion proteins

Biochem Biophys Res Commun. 2011 Jun 10;409(3):477-82. doi: 10.1016/j.bbrc.2011.05.029. Epub 2011 May 12.

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.

MeSH terms

  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / genetics
  • Amyloid beta-Peptides / toxicity*
  • Animals
  • Apoptosis
  • Cerebral Cortex / cytology
  • Maltose-Binding Proteins / chemistry
  • Maltose-Binding Proteins / genetics
  • Maltose-Binding Proteins / toxicity
  • Mice
  • Neurons / drug effects*
  • Peptide Fragments / chemistry*
  • Peptide Fragments / genetics
  • Peptide Fragments / toxicity*
  • Protein Multimerization
  • Recombinant Fusion Proteins / chemistry*
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / toxicity*
  • Saccharomyces cerevisiae / drug effects
  • Solubility

Substances

  • Amyloid beta-Peptides
  • Maltose-Binding Proteins
  • Peptide Fragments
  • Recombinant Fusion Proteins
  • amyloid beta-protein (1-42)