Abstract
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
Current Analytical Chemistry
Title:Conformations and Assembly of Amyloid Oligomers by Electrospray Ionisation - Ion Mobility Spectrometry - Mass Spectrometry
Volume: 9 Issue: 2
Author(s): Eva Illes-Toth and David P. Smith
Affiliation:
Keywords: Amyloid, ion mobility spectrometry, mass spectrometry, oligomer, protein folding, protein misfolding
Abstract: 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.
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Cite this article as:
Illes-Toth Eva and P. Smith David, Conformations and Assembly of Amyloid Oligomers by Electrospray Ionisation - Ion Mobility Spectrometry - Mass Spectrometry, Current Analytical Chemistry 2013; 9 (2) . https://dx.doi.org/10.2174/1573411011309020003
DOI https://dx.doi.org/10.2174/1573411011309020003 |
Print ISSN 1573-4110 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-6727 |
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