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Enrichment of multiphosphorylated peptides using novel magnetic TiO2 based nanomaterial

Autoři: Kupčík Rudolf | Macák Jan | Řehulka Pavel | Krulišová Pavla | Bílková Zuzana

Rok: 2015

Druh publikace: ostatní - přednáška nebo poster

Strana od-do: nestránkováno

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Jazyk	Název	Abstrakt	Klíčová slova
eng	Enrichment of multiphosphorylated peptides using novel magnetic TiO2 based nanomaterial	One of the challenges in phosphoproteomics is the enrichment and analysis of multiphosphorylated peptides. A widely used enrichment techniques for phosphopeptides utilize either metal ions e.g. Fe<sup>3+</sup> or metal oxides, e.g. TiO<sub>2</sub>. Materials made from TiO<sub>2</sub> are able to bind multiphosphorylated peptides as well as monophosphorylated peptides but elution of multiphosphorylated peptides is difficult due to their extremely high binding to TiO<sub>2</sub> material (1). The magnetic nanomaterial based on TiO<sub>2</sub> introduced in this work with different structural state significantly increases the number of eluted and analyzed multiphosphorylated peptides, as compared to common TiO<sub>2</sub> materials available today. Number of identified monophosphorylated peptides was the same for all tested materials. However, elution fractions obtained from the new magnetic nanomaterial contained significantly higher portion of multiphosphorylated peptides, as compared to commonly used commercial TiO<sub>2</sub> beads. These results indicate an improved performance in the analysis of multiphosphorylated peptides. In addition, enriched samples were obtained in a single step using only one type of carrier in comparison to SIMAC protocol. The presented magnetic nanomaterial showed the high enrichment efficiency especially for multiphosphorylated peptides that are difficult to elute from TiO<sub>2</sub> in general. Another advantage is its magnetic property making the material handling easier during all enrichment steps. All these results and properties predetermine this material as ideal tool for phosphoproteomics studies in various organisms.	phosphoproteomics, TiO2, mass spectrometry, nanomaterial

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