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Peptide Fragmentation and Surface Structural Analysis by Means of ToF-SIMS Using Large Cluster Ion Sources

Journal article
Authors Y. Yokoyama
S. Aoyagi
M. Fujii
J. Matsuo
John S. Fletcher
N. P. Lockyer
J. C. Vickerman
M. K. Passarelli
R. Havelund
M. P. Seah
Published in Analytical Chemistry
Volume 88
Issue 7
Pages 3592-3597
ISSN 0003-2700
Publication year 2016
Published at Department of Chemistry and Molecular Biology
Pages 3592-3597
Language en
Keywords mass-spectrometry, universal equation, ar cluster, argon, beams, energy, yields, size, Chemistry
Subject categories Analytical Chemistry


Peptide or protein structural analysis is crucial for the evaluation of biochips and biodevices, therefore an analytical technique with the ability to detect and identify protein and peptide species directly from surfaces with high lateral resolution is required. In this report, the efficacy of ToF-SIMS to analyze and identify proteins directly from surfaces is evaluated. Although the physics governing the SIMS bombardment process precludes the ability for researchers to detect intact protein or larger peptides of greater than a few thousand mass unit directly, it is possible to obtain information on the partial structures of peptides or proteins using low energy per atom argon duster ion beams. Large cluster ion beams, such as Ar dusters and C-60 ion beams, produce spectra similar to those generated by tandem MS. The SIMS bombardment process also produces peptide fragment ions not detected by conventional MS/MS techniques. In order to clarify appropriate measurement conditions for peptide structural analysis, peptide fragmentation dependency on the energy of a primary ion beam and ToF-SIMS specific fragment ions are evaluated. It was found that the energy range approximately 6 <= E/n <= 10 eV/atom is most effective for peptide analysis based on peptide fragments and [M + H] ions. We also observed the cleaving of side chain moieties at extremely low-energy E/n <= 4 eV/atom.

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