Enzyme-cleavable tandem peptides for quantitative studies in MS-based proteomics

Authors

  • Dominic Winter,

    1. Molecular Structure Analysis, German Cancer Research Center, Heidelberg, Germany
    Current affiliation:
    1. Institute for Biochemistry and Molecular Biology, Rheinische Friedrich-Wilhelms-University, Germany
    Search for more papers by this author
    • These authors contributed equally to this work.

  • Chien-Wen Hung,

    1. Molecular Structure Analysis, German Cancer Research Center, Heidelberg, Germany
    Current affiliation:
    1. Institute for Experimental Medicine, Christian-Albrechts-University, Germany
    Search for more papers by this author
    • These authors contributed equally to this work.

  • Thorsten W. Jaskolla,

    1. Cluster of Excellence Macromolecular Complexes, Institute of Pharmaceutical Chemistry, Goethe-University Frankfurt, Frankfurt, Germany
    Current affiliation:
    1. Institute of Medical Physics and Biophysics, University of Münster, Münster, Germany
    Search for more papers by this author
  • Michael Karas,

    1. Cluster of Excellence Macromolecular Complexes, Institute of Pharmaceutical Chemistry, Goethe-University Frankfurt, Frankfurt, Germany
    Search for more papers by this author
  • Wolf D. Lehmann

    Corresponding author
    • Molecular Structure Analysis, German Cancer Research Center, Heidelberg, Germany
    Search for more papers by this author

Correspondence: Professor Wolf D. Lehmann, Molecular Structure Analysis, German Cancer Research Center, 69120 Heidelberg, Germany

E-mail: wolf.lehmann@dkfz.de

Fax: +49-6221-424561

Abstract

A novel type of peptide standard is introduced that consists of two peptides combined in one synthetic molecule and separated by a proteolytic cleavage site. Upon enzymatic digestion, the two peptides are released in a molar one-to-one ratio. This method enables the generation of exact equimolar mixtures of two peptides of any nature and origin, thereby providing a valuable tool for the investigation of fundamental phenomena in MS. The applicability of the method is exemplified by the analysis of the effect of peptide sequence variations on the relative ionization efficiency in ESI- and MALDI-MS.

Ancillary