Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly

BBAPAP-38919; No. of pages: 12; 4C: 2, 3, 4, 6, 7, 8, 9
Biochimica et Biophysica Acta xxx (2012) xxx–xxx

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Review

Advances in ion mobility spectrometry–mass spectrometry reveal key insights into amyloid assembly☆
L.A. Woods, S.E. Radford ⁎, A.E. Ashcroft ⁎⁎
Astbury Centre for Structural Molecular Biology & School of Molecular and Cellular Biology, University of Leeds, LS2 9JT, UK

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Interfacing ion mobility spectrometry to mass spectrometry (IMS–MS) has enabled mass spectrometric analyses to extend into an extra dimension, providing unrivalled separation and structural characterization of lowly populated species in heterogeneous mixtures. One biological system that has benefitted significantly from such advances is that of amyloid formation. Using IMS–MS, progress has been made into identifying transiently populated monomeric and oligomeric species for a number of different amyloid systems and has led to an enhanced understanding of the mechanism by which small molecules modulate amyloid formation. This review highlights recent advances in this field, which have been accelerated by the commercial availability of IMS–MS instruments. This article is part of a Special Issue entitled: Mass spectrometry in structural biology. © 2012 Elsevier B.V. All rights reserved.

Article history: Received 30 July 2012 Received in revised form 27 September 2012 Accepted 2 October 2012 Available online xxxx Keywords: Amyloid Ion mobility spectrometry Mass spectrometry Oligomer Ligand binding

1. Introduction Mass spectrometry (MS) has become widely accepted as a tool to analyse biological systems over the past twenty years, subsequent to the pioneering development of electrospray ionization (ESI) [1,2]. The advent of ESI, and other soft ionization techniques such as matrix assisted laser