期刊
ACS APPLIED MATERIALS & INTERFACES
卷 7, 期 18, 页码 9563-9572出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsami.5b01006
关键词
2D nanosheet; ternary nanocomposite; phosphopeptide; enrichment; dephosphorylation
资金
- National Basic Research Program of China [2011CB933502]
- National Natural Science Foundation of China [21205060, 21335004]
- Research Fund for the Doctoral Program of Higher Education of China [20120091120029]
- Program for New Century Excellent Talents in University [NCET-12-0256]
- Deanship of Scientific Research at King Saud University through International Research Group Project [RGP-VPP-029]
Global characterization and in-depth understanding of phosphoproteome based on mass spectrometry (MS) desperately needs a highly efficient affinity probe during sample preparation. In this work, a ternary nanocornposite of magnetite/ceria-codecorated titanoniobate nanosheet (MC-TiNbNS) was synthesized by the electrostatic assembly of Fe3O4 nanospheres and in situ growth of CeO2 nanopartides on pre-exfoliated titanoniobate and eventually utilized as the probe and catalyst for the enrichment and dephosphorylation of phosphopeptides: The two-dimensional (2D) structured titanoniobate nanosheet not only promoted the efficacy of capturing phosphopeptides with enlarged surface area, but also functioned as a substrate for embracing the magnetic anchor Fe3O4 to enable magnetic separation and mimic phosphatase CeO2 to produce identifying signatures of phosphopeptides. Compared to single-component TiNbNS or CeO2 nanopartides, the ternary nanocornposite provided direct evidence of the number of phosphorylation sites while maintaining the enrichment efficiency. Moreover, by altering the on-sheet CeO2 coverage, the dephosphorylation activity could be fine-tuned, generating continuously adjustable signal intensities of both phosphopeptides and their dephosphorylated tags. Exhaustive detection of both mono- and multiphosphorylated peptides with precise counting of their phosphorylation sites was achieved in the primary mass spectra in the cases of digests of standard phosphoprotein and skim milk, as well as a more complex biological sample, human serum. With the resulting highly informative mass spectra, this multifunctional probe can be used as a promising tool for the fast and comprehensive characterization of phosphopeptides in MS-based phosphoproteomics.
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