Journal
RAPID COMMUNICATIONS IN MASS SPECTROMETRY
Volume 25, Issue 17, Pages 2468-2474Publisher
WILEY-BLACKWELL
DOI: 10.1002/rcm.5140
Keywords
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Funding
- Czech Ministry of Education [6046137305]
- Specific University Research (MSMT) [21/2011]
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In our laboratory, we have been studying the reductive processes that occur during matrix-assisted laser desorption/ionization (MALDI) experiments. Recently, we have finished an analysis of the DHB matrix effect on the azo group in cyclic peptides. However, deep understanding of disulfide bond behaviour during a mass spectrometry (MS) experiment is much more important in proteomics as its reduction can cause serious errors in protein spectra interpretation. Therefore, we have focused on Intra- and intermolecular disulfide bonds as well as disulfide bonds connecting cysteine and 2-thio-5-nitrobenzoic acid (TNB, Ellman's reagent modification) in model peptides during MALDI MS measurements. While the reduction was not observed for Intra- and intermolecular cysteine-cysteine disulfide bonds, the disulfide connection between cysteine and TNB was always affected. It was proved that TNB and Ellman's reagent can act as a matrix itself. The results obtained enabled us to propose a reaction mechanism model which is able to describe the phenomena observed during the desorption/ionization process of disulfide-containing molecules. Copyright (C) 2011 John Wiley & Sons, Ltd.
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