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- W1981601608 abstract "Tandem mass spectrometry (MS/MS) is a powerful tool for characterization of post-translationally modified proteins, including ε-N-acetyllysine-containing species. Previous reports indicate that ε-N-acetyllysine immonium ions are useful marker ions for peptides containing ε-N-acetyllysine, but the specificity and sensitivity of these ions for assignment of lysine acetylation by MS/MS have not been studied in detail. We investigated MS/MS data sets of 172 ε-N-acetyllysine tryptic peptides and 268 nonacetylated tryptic peptides to establish the utility and reliability of ε-N-acetyllysine immonium ions for identification and validation of acetylated peptides. Our analysis shows that the immonium ion at m/z 143 lacks specificity for lysine-acetylated peptides, whereas the derivative at m/z 126 is highly specific (98.1%). We also studied the positional effect of the ε-N-acetyllysine on the intensity of observed acetyllysine immonium ions. We observed an increase in acetyllysine immonium ion intensities when the acetylated lysine was N-terminally positioned in the peptide as compared to internal positions. Based on these observations we propose a validation scheme for unambiguous assignment of acetyllysine-containing peptides by MS/MS. Our analysis of ε-N-acetyllysine immonium ions provide a framework for investigation of MS/MS marker ion specificity and sensitivity that can be applied in studies of other types of post-translational modifications." @default.
- W1981601608 created "2016-06-24" @default.
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- W1981601608 date "2008-03-14" @default.
- W1981601608 modified "2023-10-17" @default.
- W1981601608 title "Utility of Immonium Ions for Assignment of ε-<i>N</i>-Acetyllysine-Containing Peptides by Tandem Mass Spectrometry" @default.
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- W1981601608 doi "https://doi.org/10.1021/ac800005n" @default.
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