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Miniaturized ultra high field asymmetric waveform ion mobility spectrometry combined with mass spectrometry for peptide analysis

journal contribution
posted on 18.09.2014 by Lauren J. Brown, Danielle E. Toutoungi, Neil A. Devenport, Jim Reynolds, G. Kaur-Atwal, P. Boyle, Colin Creaser
Miniaturized ultra high field asymmetric waveform ion mobility spectrometry (ultra-FAIMS) combined with mass spectrometry (MS) has been applied to the analysis of standard and tryptic peptides, derived from α-1-acid glycoprotein, using electrospray and nanoelectrospray ion sources. Singly and multiply charged peptide ions were separated in the gas phase using ultra-FAIMS and detected by ion trap and time-of-flight MS. The small compensation voltage (CV) window for the transmission of singly charged ions demonstrates the ability of ultra-FAIMS-MS to generate pseudo-peptide mass fingerprints that may be used to simplify spectra and identify proteins by database searching. Multiply charged ions required a higher CV for transmission, and ions with different amino acid sequences may be separated on the basis of their differential ion mobility. A partial separation of conformers was also observed for the doubly charged ion of bradykinin. Selection on the basis of charge state and differential mobility prior to tandem mass spectrometry facilitates peptide and protein identification by allowing precursor ions to be identified with greater selectivity, thus reducing spectral complexity and enhancing MS detection.

Funding

The authors would like to acknowledge Owlstone Ltd. and Loughborough University for financial support.

History

School

  • Science

Department

  • Chemistry

Published in

ANALYTICAL CHEMISTRY

Volume

82

Issue

23

Pages

9827 - 9834 (8)

Citation

BROWN, L.J. ... et al, 2010. Miniaturized ultra high field asymmetric waveform ion mobility spectrometry combined with mass spectrometry for peptide analysis. Analytical Chemistry, 82 (23), pp. 9827 - 9834.

Publisher

© American Chemical Society

Version

VoR (Version of Record)

Publisher statement

This work is made available according to the conditions of the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) licence. Full details of this licence are available at: https://creativecommons.org/licenses/by-nc-nd/4.0/

Publication date

2010

Notes

This article is closed access.

ISSN

0003-2700

Language

en

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