| Literature DB >> 26696126 |
Tristan Doussineau1, Carole Mathevon2, Lucie Altamura2, Charlotte Vendrely3,4, Philippe Dugourd1, Vincent Forge5, Rodolphe Antoine6.
Abstract
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.Keywords: amyloids; fibrils; mass spectrometry; proteins; self-assembly
Mesh:
Substances:
Year: 2015 PMID: 26696126 DOI: 10.1002/anie.201508995
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336