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- Title
Deciphering the Structure, Growth and Assembly of Amyloid-Like Fibrils Using High-Speed Atomic Force Microscopy.
- Authors
Milhiet, Pierre-Emmanuel; Yamamoto, Daisuke; Berthoumieu, Olivia; Dosset, Patrice; Le Grimellec, Christian; Verdier, Jean-Michel; Marchal, Stéphane; Ando, Toshio
- Abstract
Formation of fibrillar structures of proteins that deposit into aggregates has been suggested to play a key role in various neurodegenerative diseases. However mechanisms and dynamics of fibrillization remains to be elucidated. We have previously established that lithostathine, a protein overexpressed in the pre-clinical stages of Alzheimer's disease and present in the pathognomonic lesions associated with this disease, form fibrillar aggregates after its N-terminal truncation. In this paper we visualized, using high-speed atomic force microscopy (HS-AFM), growth and assembly of lithostathine protofibrils under physiological conditions with a time resolution of one image/s. Real-time imaging highlighted a very high velocity of elongation. Formation of fibrils via protofibril lateral association and stacking was also monitored revealing a zipper-like mechanism of association. We also demonstrate that, like other amyloid β peptides, two lithostathine protofibrils can associate to form helical fibrils. Another striking finding is the propensity of the end of a growing protofibril or fibril to associate with the edge of a second fibril, forming false branching point. Taken together this study provides new clues about fibrillization mechanism of amyloid proteins.
- Subjects
NEURODEGENERATION; MICROSCOPICAL technique; FIBER deficiency diseases; VENTRICULAR fibrillation; AMYLOID; IMAGING systems in biology
- Publication
PLoS ONE, 2010, Vol 5, Issue 10, p1
- ISSN
1932-6203
- Publication type
Article
- DOI
10.1371/journal.pone.0013240