Changes in the molecular ion yield and fragmentation of peptides under various primary ions in ToF-SIMS and matrix-enhanced ToF-SIMS

Biointerphases
Martin KörsgenHeinrich F Arlinghaus

Abstract

Time of flight secondary ion mass spectrometry (ToF-SIMS) is a powerful technique for the nanoanalysis of biological samples, but improvements in sensitivity are needed in order to detect large biomolecules, such as peptides, on the individual cell level at physiological concentrations. Two promising options to improve the sensitivity of SIMS to large peptides are the use of cluster primary ions to increase desorption of intact molecules or the use of matrix-assisted laser desorption/ionization (MALDI) matrices to increase the ionization probability. In this paper, the authors have combined these two approaches in order to improve understanding of the interaction between ionization and fragmentation processes. The peptides bradykinin and melittin were prepared as neat monolayers on silicon, in a Dextran-40 matrix and in two common MALDI matrices, 2,5-dihydroxybenzoic acid (DHB) and α-cyano-4-hydroxy cinnamic acid (HCCA). ToF-SIMS spectra of these samples were collected using a range of small Bi cluster primary ions and large Ar cluster primary ions. The trends observed in the molecular ion yield and the [M+H](+)/C4H8N(+) ratio with primary ion cluster size were sample system dependent. The molecular ion yield of the bradykinin ...Continue Reading

References

Nov 1, 1984·Biomedical Mass Spectrometry·P Roepstorff, J Fohlman
Feb 12, 2005·Journal of Mass Spectrometry : JMS·Liam A McDonnellRon M A Heeren
Aug 23, 2005·Journal of the American Society for Mass Spectrometry·David TouboulOlivier Laprévote
Nov 26, 2014·Analytical and Bioanalytical Chemistry·Felix DraudeHeinrich F Arlinghaus
Oct 1, 2015·Journal of the American Society for Mass Spectrometry·Martin KörsgenHeinrich F Arlinghaus

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