Versatile nanocomposites in phosphoproteomics: A review
[Display omitted] ► Protein phosphorylation, the most important post-translational modification. ► Enrichment of phosphopeptides for mapping protein phosphorylation sites. ► Versatile nanocomposites of different materials. ► The nanocomposites include magnetic, coated, embedded as well as chemically...
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Veröffentlicht in: | Analytica chimica acta 2012-10, Vol.747, p.7-18 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | [Display omitted]
► Protein phosphorylation, the most important post-translational modification. ► Enrichment of phosphopeptides for mapping protein phosphorylation sites. ► Versatile nanocomposites of different materials. ► The nanocomposites include magnetic, coated, embedded as well as chemically derivatized materials. ► Different base materials such as polymers, carbon based and metal oxides.
Protein phosphorylation is one of the most important post-translational modifications. Phosphorylated peptides are present in low abundance in blood serum but play a vital role in regulatory mechanisms and may serve as casual factors in diseases. The enrichment and analysis of phosphorylated peptides directly from human serum and mapping the phosphorylation sites is a challenging task. Versatile nanocomposites of different materials have been synthesized using simple but efficient methodologies for their enrichment. The nanocomposites include magnetic, coated, embedded as well as chemically derivatized materials. Different base materials such as polymers, carbon based and metal oxides are used. The comparison of nanocomposites with respective nanoparticles provides sufficient facts about their efficiency in terms of loading capacity and capture efficiency. The cost for preparing them is low and they hold great promise to be used as chromatographic materials for phosphopeptide enrichment. This review gives an overview of different nanocomposites in phosphoproteomics, discussing the improved efficiency than the individual counterparts and highlighting their significance in phosphopeptide enrichment. |
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ISSN: | 0003-2670 1873-4324 |
DOI: | 10.1016/j.aca.2012.08.004 |