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Performance of five different electrospray ionisation sources in conjunction with rapid monolithic column liquid chromatography and fast MS/MS scanning.

Burgess, K E V, Lainson, A, Imrie, L, Fraser-Pitt, Douglas J, Yaga, R, Smith, David G E, Swart, R, Pitt, A R and Inglis, Neil F (2009) Performance of five different electrospray ionisation sources in conjunction with rapid monolithic column liquid chromatography and fast MS/MS scanning. Proteomics, 9 (6). pp. 1720-1726.

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Abstract/Description

The performances of five different ESI sources coupled to a polystyrene-divinylbenzene monolithic column were compared in a series of LC-ESI-MS/MS analyses of Escherichia coli outer membrane proteins. The sources selected for comparison included two different modifications of the standard electrospray source, a commercial low-flow sprayer, a stainless steel nanospray needle and a coated glass Picotip. Respective performances were judged on sensitivity and the number and reproducibility of significant protein identifications obtained through the analysis of multiple identical samples. Data quality varied between that of a ground silica capillary, with 160 total protein identifications, the lowest number of high quality peptide hits obtained (3012), and generally peaks of lower intensity; and a stainless steel nanospray needle, which resulted in increased precursor ion abundance, the highest-quality peptide fragmentation spectra (5414) and greatest number of total protein identifications (259) exhibiting the highest MASCOT scores (average increase in score of 27.5% per identified protein). The data presented show that, despite increased variability in comparative ion intensity, the stainless steel nanospray needle provides the highest overall sensitivity. However, the resulting data were less reproducible in terms of proteins identified in complex mixtures - arguably due to an increased number of high intensity precursor ion candidates.

Item Type: Article
Electronic ISSN: 1615-9853
Uncontrolled Keywords: Electrospray ionisation; Liquid chromatography-tandem mass spectrometry; Membrane proteins; Objective evaluation;
University Divisions/Research Centres: Faculty of Health, Life & Social Sciences > School of Life, Sport and Social Sciences
Dewey Decimal Subjects: 500 Science > 570 Life sciences; biology > 572 Biochemistry
Library of Congress Subjects: Q Science > QH Natural history > QH301 Biology
Item ID: 5490
Depositing User: Dr Douglas Fraser-Pitt
Date Deposited: 22 Jun 2012 14:46
Last Modified: 01 Nov 2012 11:39
URI: http://researchrepository.napier.ac.uk/id/eprint/5490

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