Unknown

Dataset Information

0

Deciphering the structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy.


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 ß 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.

SUBMITTER: Milhiet PE 

PROVIDER: S-EPMC2951901 | biostudies-literature | 2010

REPOSITORIES: biostudies-literature

altmetric image

Publications

Deciphering the structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy.

Milhiet Pierre-Emmanuel PE   Yamamoto Daisuke D   Berthoumieu Olivia O   Dosset Patrice P   Le Grimellec Christian C   Verdier Jean-Michel JM   Marchal Stéphane S   Ando Toshio T  

PloS one 20101008 10


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  ...[more]

Similar Datasets

| S-EPMC4931465 | biostudies-literature
| S-EPMC4789755 | biostudies-literature
| S-EPMC4889376 | biostudies-literature
| S-EPMC6704188 | biostudies-literature
| S-EPMC5752618 | biostudies-literature
| S-EPMC7661283 | biostudies-literature
| S-EPMC7914567 | biostudies-literature
| S-EPMC5389415 | biostudies-literature
| S-EPMC7506678 | biostudies-literature
| S-EPMC7149427 | biostudies-literature