Eva Illes-Toth and David P. Smith Pages 165 - 180 ( 16 )
Amyloid structures accumulate and propagate through self-assembly of partially folded proteins and peptides, resulting in a range of disease states. Key to understanding amyloid disease is the characterisation of the often toxic oligomeric species formed during the early stages of fibril assembly. Electrospray ionisation- ion mobility spectrometry - mass spectrometry (ESI-IMS-MS) has emerged as a powerful tool to investigate amyloid oligomer assembly and protein conformation change. In this review we focus on the role of ESI-IMS-MS in understanding and probing conformational changes and the early stages of protein aggregation.
Amyloid, ion mobility spectrometry, mass spectrometry, oligomer, protein folding, protein misfolding
Faculty of Health and Wellbeing Sheffield Hallam University Howard Street, Sheffield S1 1WB, UK.