期刊
JOURNAL OF MASS SPECTROMETRY
卷 57, 期 3, 页码 -出版社
WILEY
DOI: 10.1002/jms.4812
关键词
AMPylation; chemical proteomics; MS-tags; protein post-translational modifications; reporter ions
资金
- Liebig fellowship from Fonds der Chemischen Industrie
- LMUexcellent Junior Fund
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) [SFB 1309]
The identification and quantification of modified peptides are important for understanding the biological function of protein modifications. This study introduces a synthesized tandem mass spectrometry tag for direct peptide-PTM quantification.
The identification and quantification of modified peptides are critical for the functional characterization of post-translational protein modifications (PTMs) to elucidate their biological function. Nowadays, quantitative mass spectrometry coupled with various bioinformatic pipelines has been successfully used for the determination of a wide range of PTMs. However, direct characterization of low abundant protein PTMs in bottom-up proteomic workflow remains challenging. Here, we present the synthesis and evaluation of tandem mass spectrometry tags (TMT) which are introduced via click-chemistry into peptides bearing alkyne handles. The fragmentation properties of the two mass tags were validated and used for screening in a model system and analysis of AMPylated proteins. The presented tags provide a valuable tool for diagnostic peak generation to increase confidence in the identification of modified peptides and potentially for direct peptide-PTM quantification from various experimental conditions.
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