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Electron capture dissociation product ion abundances at the X amino acid in RAAAA-X-AAAAK peptides correlate with amino acid polarity and radical stability

Vorobyev, Aleksey ; Hamidane, Hisham ; Tsybin, Yury

In: Journal of the American Society for Mass Spectrometry, 2009, vol. 20, no. 12, p. 2273-2283

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    Title
    • Electron capture dissociation product ion abundances at the X amino acid in RAAAA-X-AAAAK peptides correlate with amino acid polarity and radical stability
    Author
    • Vorobyev, Aleksey. Biomolecular Mass Spectrometry Laboratory, Ecole Polytechnique Fédérale de Lausanne, BCH 4307, 1015, Lausanne, Switzerland
    • Hamidane, Hisham. Biomolecular Mass Spectrometry Laboratory, Ecole Polytechnique Fédérale de Lausanne, BCH 4307, 1015, Lausanne, Switzerland
    • Tsybin, Yury. Biomolecular Mass Spectrometry Laboratory, Ecole Polytechnique Fédérale de Lausanne, BCH 4307, 1015, Lausanne, Switzerland
    Document Type
    • Postprint
    Language
    • English
    Published in
    • Journal of the American Society for Mass Spectrometry, 2009, vol. 20, no. 12, p. 2273-2283. Springer-Verlag
    Other Version
    Classification
    • Chemistry
    OAI-PMH Identifier
    • oai:doc.rero.ch:311384
    Summary
    We present mechanistic studies aimed at improving the understanding of the product ion formation rules in electron capture dissociation (ECD) of peptides and proteins in Fourier transform ion cyclotron resonance mass spectrometry. In particular, we attempted to quantify the recently reported general correlation of ECD product ion abundance (PIA) with amino acid hydrophobicity. The results obtained on a series of model H-RAAAAXAAAAK-OH peptides confirm a direct correlation of ECD PIA with X amino acid hydrophobicity and polarity. The correlation factor (R) exceeds 0.9 for 12 amino acids (Ile, Val, His, Asn, Asp, Glu, Gln, Ser, Thr, Gly, Cys, and Ala). The deviation of ECD PIA for seven outliers (Pro is not taken into consideration) is explained by their specific radical stabilization properties (Phe, Trp, Tyr, Met, and Leu) and amino acid basicity (Lys, Arg). Phosphorylation of Ser, Thr, and Tyr decreases the efficiency of ECD around phosphorylated residues, as expected. The systematic arrangement of amino acids reported here indicates a possible route toward development of a predictive model for quantitative electron capture/transfer dissociation tandem mass spectrometry, with possible applications in proteomics