1. Capturing Aβ42 aggregation in the cell.
- Author
-
Bemporad F, Cecchi C, and Chiti F
- Subjects
- Amyloid beta-Peptides ultrastructure, Humans, Peptide Fragments ultrastructure, Amyloid beta-Peptides chemistry, Microscopy, Confocal methods, Peptide Fragments chemistry, Protein Multimerization
- 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., Competing Interests: The authors declare that they have no conflicts of interest with the contents of this article., (© 2019 Bemporad et al.)
- Published
- 2019
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