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

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.

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