Capturing Aβ42 aggregation in the cell

• Published in: Journal of Biological Chemistry
• Main Authors: Bemporad, Francesco, Cecchi, Cristina, Chiti, Fabrizio
• Format: Text
• Language: English
• Published: American Society for Biochemistry and Molecular Biology 2019
• Subjects: Editors' Picks Highlights; Arctic
• Online Access: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6364781/; http://www.ncbi.nlm.nih.gov/pubmed/30710006; https://doi.org/10.1074/jbc.H119.007392

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.