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Title: Miniaturized ultra high field asymmetric waveform ion mobility spectrometry combined with mass spectrometry for peptide analysis
Authors: Brown, Lauren J.
Toutoungi, Danielle E.
Devenport, Neil A.
Reynolds, James C.
Kaur-Atwal, G.
Boyle, P.
Creaser, Colin S.
Issue Date: 2010
Publisher: © American Chemical Society
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.
Abstract: 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.
Description: This article is closed access.
Sponsor: The authors would like to acknowledge Owlstone Ltd. and Loughborough University for financial support.
Version: Published
DOI: 10.1021/ac102125u
URI: https://dspace.lboro.ac.uk/2134/15894
Publisher Link: http://dx.doi.org/10.1021/ac102125u
ISSN: 0003-2700
Appears in Collections:Closed Access (Chemistry)

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