Mass Determination of Entire Amyloid Fibrils by Using Mass Spectrometry

Amyloid fibrils are self‐assembled protein structures with important roles in biology (either pathogenic or physiological), and are attracting increasing interest in nanotechnology. However, because of their high aspect ratio and the presence of some polymorphism, that is, the possibility to adopt v...

Full description

Saved in:
Bibliographic Details
Published in:Angewandte Chemie 2016-02, Vol.128 (7), p.2386-2390
Main Authors: Doussineau, Tristan, Mathevon, Carole, Altamura, Lucie, Vendrely, Charlotte, Dugourd, Philippe, Forge, Vincent, Antoine, Rodolphe
Format: Article
Language:English
Subjects:
Amyloide
Biology
Chemistry
Fibrillen
Fibrils
High aspect ratio
Information dissemination
Mass spectrometry
Mass spectroscopy
Massenspektrometrie
Nanotechnology
Physiology
Polymorphism
Proteine
Proteins
Scientific imaging
Selbstorganisation
Viruses
Water analysis
β-Amyloid
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Amyloid fibrils are self‐assembled protein structures with important roles in biology (either pathogenic or physiological), and are attracting increasing interest in nanotechnology. However, because of their high aspect ratio and the presence of some polymorphism, that is, the possibility to adopt various structures, their characterization is challenging and basic information such as their mass is unknown. Here we show that charge‐detection mass spectrometry, recently developed for large self‐assembled systems such as viruses, provides such information in a straightforward manner. Massenbestimmung modern: Das große Seitenverhältnis von Amyloidfibrillen und eine gewisse Polymorphie haben zur Folge, dass diese selbstorganisierten Proteinstrukturen nur schwierig zu charakterisieren sind und Basisinformationen wie ihre Masse unbekannt sind. Mithilfe der Ladungsermittlungs‐Massenspektrometrie (CDMS) sind solche Informationen einfach zugänglich, was ein Verfolgen der Proteinaggregation in Echtzeit ermöglicht.
ISSN:0044-8249
1521-3757
DOI:10.1002/ange.201508995