期刊
INTERNATIONAL JOURNAL OF MASS SPECTROMETRY
卷 287, 期 1-3, 页码 77-86出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijms.2008.08.020
关键词
Nitrotyrosine-containing peptide; MALDI-induced fragmentation; Nitro-Tyr-leucine enkephalin; d(5)-Phe-Nitro-Tyr-leucine enkephalin; Sensitivity
资金
- Chiesi Pharmaceuticals (Parma, Italy)
- NIH [RR016679]
The long-term objective of this study is to use MALDI MS and MS/MS to study the fragmentation pattern of in vitro nitrotyrosine-containing peptides in order to assist the interpretation of MS-identification of endogenous nitroproteins in human tissues and fluids. The short-term objective is to study synthetic leucine enkephalin, nitro-Tyr-leucine enkephalin, and d(5)-Phe-nitro-Tyr-leucine enkephalin with a vacuum matrix-assisted laser desorption/ionization linear ion-trap mass spectrometer (vMALDI-LTQ). The results demonstrated the UV laser-induced photochemical decomposition of the nitro group. Although photochemical decomposition decreased the ion intensity and complicated the MS spectrum, the recognition of that unique decomposition pattern unambiguously identified a nitrotyrosine. The a(4)- and b(4)-ions were the most intense fragment ions found in the MS/MS spectra for those three synthetic peptides. Compared to the unmodified peptides, more collision energy optimized the fragmentation of the nitropeptide, increased the intensity of the a(4)-ion, and decreased the intensity of the b(4)-ion. Optimized laser fluence maximized the fragmentation of the nitropeptide. MS3 analysis confirmed the MS2-derived amino acid sequence, but required much more sample. To detect a nitropeptide, the sensitivity of vMALDI-LTQ is 1 fmol for MS detection and 10 fmol for MS2 detection; the S/N ratio was ca. 50:1 in those studies. Those data are important for an analysis of low-abundance endogenous nitroproteins, where preferential enrichment of nitroproteins and optimized mass spectrometry parameters are used. (C) 2008 Elsevier B.V. All rights reserved.
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