Conformations and Assembly of Amyloid Oligomers by Electrospray Ionisation - Ion Mobility Spectrometry - Mass Spectrometry

Author(s): Eva Illes-Toth, David P. Smith

Journal Name: Current Analytical Chemistry

Volume 9 , Issue 2 , 2013

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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.

Keywords: Amyloid, ion mobility spectrometry, mass spectrometry, oligomer, protein folding, protein misfolding

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Article Details

Year: 2013
Page: [165 - 180]
Pages: 16
DOI: 10.2174/1573411011309020003

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PDF: 18