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Mass Determination of Entire Amyloid Fibrils by Using Mass Spectrometry
Author(s) -
Doussineau Tristan,
Mathevon Carole,
Altamura Lucie,
Vendrely Charlotte,
Dugourd Philippe,
Forge Vincent,
Antoine Rodolphe
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201508995
Subject(s) - amyloid fibril , mass spectrometry , characterization (materials science) , fibril , chemistry , nanotechnology , amyloid (mycology) , biophysics , computational biology , materials science , amyloid β , biology , biochemistry , chromatography , disease , medicine , inorganic chemistry , pathology
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.