Mass spectrometry and the amyloid problem--how far can we go in the gas phase?
A number of proteins are capable of converting from their soluble, monomeric form into highly-ordered, insoluble aggregates known as amyloid fibrils. In vivo, these fibrils, which accumulate in organs and tissues, are associated with a wide range of amyloid diseases for which there are currently no therapeutic solutions. The molecular details of the pathway from native monomer through oligomeric intermediates to the final amyloid fibril remain a challenging enigma. Over the past few years, mass spectrometry has been applied to investigate the various stages of amyloid fibril formation, and this report summarizes the key steps achieved to date.
Ashcroft
Alison E
AE
Astbury Centre for Structural Molecular Biology, Institute of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom. a.e.ashcroft@leeds.ac.uk
D000544:Alzheimer Disease; D000682:Amyloid / Q000737:chemistry / Q000378:metabolism; D005740:Gases / Q000737:chemistry; D013058:Mass Spectrometry / Q000379:methods*; D055503:Protein Multimerization; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D057165:Proteostasis Deficiencies
D000682:Amyloid; D005740:Gases; D011506:Proteins