期刊
JOURNAL OF CHROMATOGRAPHY A
卷 1498, 期 -, 页码 56-63出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.chroma.2016.10.054
关键词
Metal-organic frameworks; Monolithic capillary; Phosphopeptides; Sample treatment; Protein phosphorylation
资金
- National Science Fund for Distinguished Young Scholars from the National Natural Science Foundation of China [21425520]
- Key Grant of 973 Program from the Ministry of Science and Technology of China [2013CB911202]
Protein phosphorylation is a major post-translational modification, which plays a vital role in cellular signaling of numerous biological processes. Mass spectrometry (MS) has been an essential tool for the analysis of protein phosphorylation, for which it is a key step to selectively enrich phosphopeptides from complex biological samples. In this study, metal-organic frameworks (MOFs)-based monolithic capillary has been successfully prepared as an effective sorbent for the selective enrichment of phosphopeptides and has been off-line coupled with matrix-assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOF MS) for efficient analysis of phosphopeptides. Using s-casein as a representative phosphoprotein, efficient phosphorylation analysis by this off-line platform was verified. Phosphorylation analysis of a nonfat milk sample was also demonstrated. Through introducing large surface areas and highly ordered pores of MOFs into monolithic column, the MOFs-based monolithic capillary exhibited several significant advantages, such as excellent selectivity toward phosphopeptides, superb tolerance to interference and simple operation procedure. Because of these highly desirable properties, the MOFs-based monolithic capillary could be a useful tool for protein phosphorylation analysis. (C) 2016 Elsevier B.V. All rights reserved.
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