Unknown

Dataset Information

0

Mass and charge distributions of amyloid fibers involved in neurodegenerative diseases: mapping heterogeneity and polymorphism.


ABSTRACT: Heterogeneity and polymorphism are generic features of amyloid fibers with some important effects on the related disease development. We report here the characterization, by charge detection mass spectrometry, of amyloid fibers made of three polypeptides involved in neurodegenerative diseases: A?1-42 peptide, tau and ?-synuclein. Beside the mass of individual fibers, this technique enables to characterize the heterogeneity and the polymorphism of the population. In the case of A?1-42 peptide and tau protein, several coexisting species could be distinguished and characterized. In the case of ?-synuclein, we show how the polymorphism affects the mass and charge distributions.

SUBMITTER: Pansieri J 

PROVIDER: S-EPMC5914292 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Mass and charge distributions of amyloid fibers involved in neurodegenerative diseases: mapping heterogeneity and polymorphism.

Pansieri Jonathan J   Halim Mohammad A MA   Vendrely Charlotte C   Dumoulin Mireille M   Legrand François F   Sallanon Marcelle Moulin MM   Chierici Sabine S   Denti Simona S   Dagany Xavier X   Dugourd Philippe P   Marquette Christel C   Antoine Rodolphe R   Forge Vincent V  

Chemical science 20180205 10


Heterogeneity and polymorphism are generic features of amyloid fibers with some important effects on the related disease development. We report here the characterization, by charge detection mass spectrometry, of amyloid fibers made of three polypeptides involved in neurodegenerative diseases: Aβ<sub>1-42</sub> peptide, tau and α-synuclein. Beside the mass of individual fibers, this technique enables to characterize the heterogeneity and the polymorphism of the population. In the case of Aβ<sub>  ...[more]

Similar Datasets

| S-EPMC8289188 | biostudies-literature
| S-EPMC8520725 | biostudies-literature
| S-EPMC9932299 | biostudies-literature
| S-EPMC8641661 | biostudies-literature
2022-01-11 | PXD026306 | Pride
| S-EPMC8468037 | biostudies-literature
| S-EPMC1736363 | biostudies-other
| S-EPMC10711260 | biostudies-literature
2011-01-29 | E-GEOD-26927 | biostudies-arrayexpress
| S-EPMC9455244 | biostudies-literature