期刊
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
卷 22, 期 7, 页码 1224-1233出版社
SPRINGER
DOI: 10.1007/s13361-011-0131-y
关键词
Hydrogen-accepting matrix; Matrix-assisted laser desorption/ionization; In-source decay; Phosphorylated peptides
资金
- Japan Ministry of Education, Culture, Sports, and Technology [20550081]
- Grants-in-Aid for Scientific Research [11J10272, 20550081] Funding Source: KAKEN
The use of 5-formylsalicylic acid (5-FSA) and 5-nitrosalicylic acid (5-NSA) as novel matrices for in-source decay (ISD) of peptides in matrix-assisted laser desorption/ionization (MALDI) is described. The use of 5-FSA and 5-NSA generated a-and x-series ions accompanied by oxidized peptides [M - 2 H + H](+). The preferential formation of a-and x-series ions was found to be dependent on the hydrogen-accepting ability of matrix. The hydrogen-accepting ability estimated from the ratio of signal intensity of oxidized product [M - 2 H + H](+) to that of non-oxidized protonated molecule [M + H](+) of peptide was of the order 5-NSA>5-FSA>5-aminosalicylic acid (5-ASA). 2,5-dihydroxyl benzoic acid (2,5-DHB). 0. The results suggest that the hydrogen transfer reaction from peptide to 5-FSA and 5-NSA occurs during the MALDIISD processes. The hydrogen abstraction from peptides results in the formation of oxidized peptides containing a radical site on the amide nitrogen with subsequent radical-induced cleavage at the C-alpha - C bond, leading to the formation of a- and x-series ions. The most significant feature of MALDI-ISD with 5-FSA and 5-NSA is the specific cleavage of the C-alpha - C bond of the peptide backbone without degradation of side-chain and post-translational modifications (PTM). The matrix provides a useful complementary method to conventional MALDI-ISD for amino acid sequencing and site localization of PTMs in peptides.
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