Capturing Aβ42 aggregation in the cell

J Biol Chem. 2019 Feb 1;294(5):1488-1489. doi: 10.1074/jbc.H119.007392.

Abstract

Novel imaging techniques with ever-increasing resolution are invaluable tools for the study of protein deposition, as they allow the self-assembly of proteins to be directly investigated in living cells. For the first time, the acceleration in Aβ42 aggregation induced by the Arctic mutation was monitored in cells, revealing a number of distinct morphologies that form sequentially. This approach will help discriminate the impacts of mutations on amyloid protein processing, Aβ aggregation propensity, and other mechanistic outcomes.

MeSH terms

  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / ultrastructure
  • Humans
  • Microscopy, Confocal / methods*
  • Peptide Fragments / chemistry*
  • Peptide Fragments / ultrastructure
  • Protein Multimerization*

Substances

  • Amyloid beta-Peptides
  • Peptide Fragments
  • amyloid beta-protein (1-42)