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Minimally permutated peptide analogs as internal standards for relative and absolute quantification of peptides and proteins

Authors

  • Dominic Winter,

    1. Molecular Structure Analysis, German Cancer Research Center, Heidelberg, Germany
    Current affiliation:
    1. Department of Pathology, Harvard Medical School and Children's Hospital, Boston, MA, USA
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    • These authors have contributed equally to this work.

  • Joerg Seidler,

    1. Molecular Structure Analysis, German Cancer Research Center, Heidelberg, Germany
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    • These authors have contributed equally to this work.

  • Dominik Kugelstadt,

    1. Department of Infectious Diseases, Parasitology, University Hospital Heidelberg, Heidelberg, Germany
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  • Bianca Derrer,

    1. Department of Infectious Diseases, Parasitology, University Hospital Heidelberg, Heidelberg, Germany
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  • Barbara Kappes,

    1. Department of Infectious Diseases, Parasitology, University Hospital Heidelberg, Heidelberg, Germany
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  • Wolf D. Lehmann

    Corresponding author
    1. Molecular Structure Analysis, German Cancer Research Center, Heidelberg, Germany
    • Molecular Structure Analysis (W160), German Cancer Research Center, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany Fax: +49-6221-42-45-61
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Abstract

A novel type of isobaric internal peptide standard for quantitative proteomics is described. The standard is a synthetic peptide derived from the target peptide by positional permutation of two amino acids. This type of internal standard is denominated minimally permutated peptide analog (MIPA). MIPA can be differentiated from their target analytes by LC-MS due to individual retention times and/or by MS/MS due to specific fragment ions. Both quantification methods are demonstrated using peptide mixtures of low and high complexity.

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