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Disulfide bond decay during matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry experiments
Author(s) -
Krásný Lukáš,
Hynek Radovan,
Kodíček Milan
Publication year - 2011
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.5140
Subject(s) - chemistry , mass spectrometry , reagent , cysteine , matrix assisted laser desorption/ionization , desorption , matrix (chemical analysis) , mass spectrum , molecule , combinatorial chemistry , chromatography , organic chemistry , adsorption , enzyme
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 © 2011 John Wiley & Sons, Ltd.