期刊
JOURNAL OF MASS SPECTROMETRY
卷 52, 期 2, 页码 127-131出版社
WILEY
DOI: 10.1002/jms.3906
关键词
in-source decay; hydrogen atom donor; thiol; MALDI matrix; number of disulfide bonds
资金
- JSPS KAKENHI [JP26505016]
- Nanotechnology Platform Program of the Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan
- Grants-in-Aid for Scientific Research [26505016] Funding Source: KAKEN
The ability of a thiol-containing molecule, thiosalicylic acid (TSA), to function as a reactive matrix for matrix-assisted laser desorption/ionization (MALDI) mass spectrometry analysis of peptides has been investigated. Although TSA has reducing characteristics, the use of TSA did not cause a reduction-induced MALDI in-source decay, probably because of the weak interactions between the thiol group in TSA and the carboxyl oxygen in the peptide. In contrast, when peptides containing disulfide bonds were analyzed by MALDI with TSA as the matrix, the disulfide bond was partially cleaved owing to the reaction with TSA, producing TSA-adducted peptides. The reaction between the disulfide bond and TSA was suggested to be occurred in solution. The comparison of the MALDI mass spectra obtained using conventional matrix and TSA allows us to count the number of disulfide bonds in the peptides. Copyright (C) 2017 John Wiley & Sons, Ltd.
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