Grazing incidence surface-induced dissociation of protonated peptides generated by matrix-assisted laser desorption/ionization.
The grazing incidence surface-induced dissociation (GI-SID) of various protonated peptides with typical kinetic energies of 350 eV was investigated. Peptide ions were generated by matrix-assisted laser desorption/ionization (MALDI) using delayed extraction. The collision target surfaces used were aluminum and a liquid film of perfluorinated hydrocarbons. All peptides studied in these experiments showed enhanced fragment ion yields at grazing incidence (GI-SID effect) as observed in our former experiments with other precursor ion types. In general the GI-SID spectra exhibit N-terminal a(1)-type fragment ions, immonium ions and side-chain fragment ions in the low mass-to-charge region. Fragment ion series of the peptide backbone were not observed, which are typical and abundant in the spectra of established fragmentation techniques like collision-induced dissociation, MALDI post-source decay or surface-induced dissociation at steeper angles. The potential of the GI-SID process to yield useful information for primary structure determination of peptides is indicated by the observed differences in the GI-SID spectra of the isomeric dipeptides LR and IR.
Wieghaus
A
A
Department of Chemistry, Philipps-University Marburg, D-35032 Marburg, Germany.
Schmidt
L
L
Popova
A M
AM
Komarov
V V
VV
Jungclas
H
H
D000465:Algorithms; D002138:Calibration; D002142:Californium; D004151:Dipeptides / Q000737:chemistry; D009842:Oligopeptides / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D011522:Protons; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013499:Surface Properties
D004151:Dipeptides; D009842:Oligopeptides; D010455:Peptides; D011522:Protons; D002142:Californium