4.5 Article

A Novel Approach to Collision-Induced Dissociation (CID) for Ion Mobility-Mass Spectrometry Experiments

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AMER CHEMICAL SOC
DOI: 10.1016/j.jasms.2008.11.026

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  1. U.S. Department of Energy, Division of Chemical Sciences/BES [DEFG-04ER-15,520]
  2. National Science Foundation-Major Research Instrumentation [CHE-0521216]
  3. Robert A. Welch Foundation [A-1176]
  4. Div Of Biological Infrastructure
  5. Direct For Biological Sciences [0821700] Funding Source: National Science Foundation

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Collision induced dissociation (CID) combined with matrix assisted laser desorption ionizationion mobility-mass spectrometry (MALDI-IM-MS) is described. In this approach, peptide ions are separated on the basis of mobility in a 15 cm drift cell. Following mobility separation, the ions exit the drift cell and enter a 5 cm vacuum interface with a high field region (LIP to 1000 V/CM) to undergo collisional activation. Ion transmission and ion kinetic energies in the interface are theoretically evaluated accounting for the pressure gradient, interface dimensions, and electric fields. Using this CID technique, we have successfully fragmented and sequenced a number of model peptide ions as well as peptide ions obtained by a tryptic digest. This instrument configuration allows for the Simultaneous determination of peptide mass, peptide-ion sequence, and collision-cross section of MALDI-generated ions, providing information critical to the identification of unknown components in complex proteomic samples. (J Am Soc Mass Spectrom 2009, 20, 907-914) (C) 2009 American Society for Mass Spectrometry

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