Ion mobility tandem mass spectrometry enhances performance of bottom-up proteomics

Mol Cell Proteomics. 2014 Dec;13(12):3709-15. doi: 10.1074/mcp.M114.041038. Epub 2014 Aug 8.

Abstract

One of the limiting factors in determining the sensitivity of tandem mass spectrometry using hybrid quadrupole orthogonal acceleration time-of-flight instruments is the duty cycle of the orthogonal ion injection system. As a consequence, only a fraction of the generated fragment ion beam is collected by the time-of-flight analyzer. Here we describe a method utilizing postfragmentation ion mobility spectrometry of peptide fragment ions in conjunction with mobility time synchronized orthogonal ion injection leading to a substantially improved duty cycle and a concomitant improvement in sensitivity of up to 10-fold for bottom-up proteomic experiments. This enabled the identification of 7500 human proteins within 1 day and 8600 phosphorylation sites within 5 h of LC-MS/MS time. The method also proved powerful for multiplexed quantification experiments using tandem mass tags exemplified by the chemoproteomic interaction analysis of histone deacetylases with Trichostatin A.

MeSH terms

  • Flow Injection Analysis
  • HeLa Cells
  • Histone Deacetylase Inhibitors / chemistry
  • Histone Deacetylases / analysis*
  • Humans
  • Hydroxamic Acids / chemistry
  • Ions
  • Peptide Fragments / analysis*
  • Phosphoproteins / analysis*
  • Phosphorylation
  • Proteomics / instrumentation*
  • Proteomics / methods
  • Sensitivity and Specificity
  • Tandem Mass Spectrometry / instrumentation*
  • Tandem Mass Spectrometry / methods
  • Time Factors
  • Trypsin / chemistry

Substances

  • Histone Deacetylase Inhibitors
  • Hydroxamic Acids
  • Ions
  • Peptide Fragments
  • Phosphoproteins
  • trichostatin A
  • Trypsin
  • Histone Deacetylases