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MALDI versus ESI: The Impact of the Ion Source on Peptide Identification.
Journal article

MALDI versus ESI: The Impact of the Ion Source on Peptide Identification.

  • Nadler WM German Cancer Research Center and HI-STEM gGmbH , Im Neuenheimer Feld 280, 69120 Heidelberg, Germany.
  • Waidelich D SCIEX Germany GmbH , Landwehrstraße 54, 64293 Darmstadt, Germany.
  • Kerner A German Cancer Research Center and HI-STEM gGmbH , Im Neuenheimer Feld 280, 69120 Heidelberg, Germany.
  • Hanke S German Cancer Research Center and HI-STEM gGmbH , Im Neuenheimer Feld 280, 69120 Heidelberg, Germany.
  • Berg R Department of Chemistry, University of Zurich , Winterthurerstr. 190, 8057 Zurich, Switzerland.
  • Trumpp A German Cancer Research Center and HI-STEM gGmbH , Im Neuenheimer Feld 280, 69120 Heidelberg, Germany.
  • Rösli C German Cancer Research Center and HI-STEM gGmbH , Im Neuenheimer Feld 280, 69120 Heidelberg, Germany.
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  • 2017-02-09
Published in:
  • Journal of proteome research. - 2017
ESI
MALDI
ionization
peptide modification
proteomics
Amino Acids
Cell Line
Cell Line, Tumor
Humans
Hydrophobic and Hydrophilic Interactions
Pancreas
Peptides
Proteomics
Spectrometry, Mass, Electrospray Ionization
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
English For mass spectrometry-based proteomic analyses, electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) are the commonly used ionization techniques. To investigate the influence of the ion source on peptide detection in large-scale proteomics, an optimized GeLC/MS workflow was developed and applied either with ESI/MS or with MALDI/MS for the proteomic analysis of different human cell lines of pancreatic origin. Statistical analysis of the resulting data set with more than 72 000 peptides emphasized the complementary character of the two methods, as the percentage of peptides identified with both approaches was as low as 39%. Significant differences between the resulting peptide sets were observed with respect to amino acid composition, charge-related parameters, hydrophobicity, and modifications of the detected peptides and could be linked to factors governing the respective ion yields in ESI and MALDI.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/41762
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