TY - JOUR
T1 - A Novel Approach to Collision-Induced Dissociation (CID) for Ion Mobility-Mass Spectrometry Experiments
AU - Becker, Christopher
AU - Fernandez-Lima, Francisco A.
AU - Gillig, Kent J.
AU - Russell, William K.
AU - Cologna, Stephanie M.
AU - Russell, David H.
N1 - Funding Information:
The authors acknowledge support for this research by the U.S. Department of Energy, Division of Chemical Sciences/BES (DE-FG-04ER-15,520), the National Science Foundation-Major Research Instrumentation Grant (CHE-0521216), and the Robert A. Welch Foundation (A-1176). The authors also acknowledge many helpful discussions with Tom Egan and Al Schultz at IonWerks, Inc., Houston, Texas.
PY - 2009/6
Y1 - 2009/6
N2 - Collision induced dissociation (CID) combined with matrix assisted laser desorption ionization-ion 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 (up 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.
AB - Collision induced dissociation (CID) combined with matrix assisted laser desorption ionization-ion 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 (up 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.
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U2 - 10.1016/j.jasms.2008.11.026
DO - 10.1016/j.jasms.2008.11.026
M3 - Article
C2 - 19135385
AN - SCOPUS:67349269894
SN - 1044-0305
VL - 20
SP - 907
EP - 914
JO - Journal of the American Society for Mass Spectrometry
JF - Journal of the American Society for Mass Spectrometry
IS - 6
ER -