MALDI versus ESI: The Impact of the Ion Source on Peptide Identification
journal contributionposted on 08.02.2017, 00:00 authored by Wiebke Maria Nadler, Dietmar Waidelich, Alexander Kerner, Sabrina Hanke, Regina Berg, Andreas Trumpp, Christoph Rösli
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.
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proteomic analysischarge-related parameterselectrospray ionizationion yieldsionization techniquesacid compositionpeptide setspeptide detectionStatistical analysisPeptide Identificationpancreatic originmass spectrometry-based proteomic analysescell lines72 000 peptidesESIMALDI72 000ion sourceIon Source