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Miniaturized ultra high field asymmetric waveform ion mobility spectrometry combined with mass spectrometry for peptide analysis
journal contribution
posted on 2014-09-18, 14:30 authored by Lauren J. Brown, Danielle E. Toutoungi, Neil A. Devenport, Jim ReynoldsJim Reynolds, G. Kaur-Atwal, P. Boyle, Colin CreaserMiniaturized 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 CHEMISTRYVolume
82Issue
23Pages
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 SocietyVersion
- 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
2010Notes
This article is closed access.ISSN
0003-2700Publisher version
Language
- en