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A Neutral Loss Activation Method for Improved Phosphopeptide Sequence Analysis by Quadrupole Ion Trap Mass Spectrometry

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Download Hi-Res ImageDownload to MS-PowerPointCite This:Anal. Chem. 2004, 76, 13, 3590-3598
    Article

    A Neutral Loss Activation Method for Improved Phosphopeptide Sequence Analysis by Quadrupole Ion Trap Mass Spectrometry
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    Department of Chemistry, University of Virginia, McCormick Road, Charlottesville, Virginia 22901, Department of Pathology, University of Virginia, Charlottesville, Virginia 22901, and Thermo Electron Corporation, 355 River Oaks Parkway, San Jose, California
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    Analytical Chemistry

    Cite this: Anal. Chem. 2004, 76, 13, 3590–3598
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    https://doi.org/10.1021/ac0497104
    Published May 18, 2004
    Copyright © 2004 American Chemical Society
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    Abstract

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    Recent advances in phosphopeptide enrichment prior to mass spectrometric analysis show genuine promise for characterization of phosphoproteomes. Tandem mass spectrometry of phosphopeptide ions, using collision-activated dissociation (CAD), often produces product ions dominated by the neutral loss of phosphoric acid. Here we describe a novel method, termed Pseudo MSn, for phosphopeptide ion dissociation in quadrupole ion trap mass spectrometers. The method induces collisional activation of product ions, those resulting from neutral loss(es) of phosphoric acid, following activation of the precursor ion. Thus, the principal neutral loss product ions are converted into a variety of structurally informative species. Since product ions from both the original precursor activation and all subsequent neutral loss product activations are simulataneously stored, the method generates a “composite” spectrum containing fragments derived from multiple precursors. In comparison to analysis by conventional MS/MS (CAD), Pseudo MSn shows improved phosphopeptide ion dissociation for 7 out of 10 synthetic phosphopeptides, as judged by an automated search algorithm (TurboSEQUEST). A similar overall improvement was observed upon application of Pseudo MSn to peptides generated by enzymatic digestion of a single phosphoprotein. Finally, when applied to a complex phosphopeptide mixture, several phosphopeptides misassigned by TurboSEQUEST under the conventional CAD approach were successfully identified after analysis by Pseudo MSn.

    Copyright © 2004 American Chemical Society

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    †

     Department of Chemistry, University of Virginia.

    §

     ThermoElectron Corporation.

    ‡

     Department of Pathology, University of Virginia.

    *

     To whom correspondence should be addressed. E-mail:  [email protected].

    Cited By

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    This article is cited by 330 publications.

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    Analytical Chemistry

    Cite this: Anal. Chem. 2004, 76, 13, 3590–3598
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    https://doi.org/10.1021/ac0497104
    Published May 18, 2004
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