Univerzita Pardubice Fakulta chemicko- technologická

Univerzita Pardubice

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Publikace detail

Improved enrichment of multiphosphorylated peptides suitable for tau protein analysis

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

Rok: 2015

Druh publikace: ostatní - přednáška nebo poster

Strana od-do: nestránkováno

Tituly:

Jazyk	Název	Abstrakt	Klíčová slova
eng	Improved enrichment of multiphosphorylated peptides suitable for tau protein analysis	One of the challenges in phosphoproteomics is the separation and analysis of multiply phosphorylated peptides. A widely used enrichment technique for phosphorylated peptides is technique utilizing the metal oxides, i.e. TiO2. TiO2 materilals are able to bind multiply or monophosphorylated peptides but the efficient elution of them is difficult due to the high binding affinity. Main aim is to introduce the novel nanomaterial based on TiO2 which can increase the number of multiphosphorylated peptides and separate them from monophosphorylated peptides. Material and protocol should be able to increase identifications of phosphorylated aminoacids on tau protein. TiO2 nanofibers, microparticles and magnetic nanorpaticles in combination with new elution system are charachterized with binding selectivity and elution ability. Available not only for monophosphorylated peptides but also for multiply phosphorylated peptides. Two step elution system is capable to divide phosphopeptides into two fractions mainly for magnetic nanoparticles. First elution solution elutes mostly monophophorylated peptides and small amount of multiply phosphorylated peptides. Second fraction which included multiply phosphorylated peptides had been eluted with novel elution solution. It is suitable to enrich and analyse more multiply phosphorylated peptides, which should be useful for analysis of (hyper)phosphorylated tau protein where presence of these type of peptides is presumed.	TiO2, mass spectrometry, phosphoproteomics, nanomaterials