A novel approach to collision-induced dissociation (CID) for ion mobility-mass spectrometry experiments.
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.
Becker
Christopher
C
The Laboratory for Biological Mass Spectrometry, Department of Chemistry, Texas A and M University, College Station, Texas 77843-3255, USA.
Fernandez-Lima
Francisco A
FA
Gillig
Kent J
KJ
Russell
William K
WK
Cologna
Stephanie M
SM
Russell
David H
DH
D003198:Computer Simulation; D004867:Equipment Design; D005344:Fibrinopeptide A / Q000378:metabolism; D008956:Models, Chemical; D010446:Peptide Fragments / Q000737:chemistry* / Q000302:isolation & purification; D011312:Pressure; D011506:Proteins / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D014357:Trypsin / Q000378:metabolism
D010446:Peptide Fragments; D011506:Proteins; D005344:Fibrinopeptide A; D014357:Trypsin