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In-situ enrichment of phosphopeptides on MALDI plates modified by ambient ion landing
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SYSNO ASEP 0382652 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title In-situ enrichment of phosphopeptides on MALDI plates modified by ambient ion landing Author(s) Krásný, Lukáš (MBU-M) RID
Pompach, Petr (MBU-M) RID, ORCID
Strohalm, Martin (MBU-M)
Obšilová, Veronika (FGU-C) RID, ORCID, SAI
Strnadová, Marcela (MBU-M)
Novák, Petr (MBU-M) RID, ORCID
Volný, Michael (MBU-M) ORCIDSource Title Journal of Mass Spectrometry. - : Wiley - ISSN 1076-5174
Roč. 47, č. 10 (2012), s. 1294-1302Number of pages 12 s. Language eng - English Country GB - United Kingdom Keywords MALDI FTICR ; phosphopetides ; enrichment Subject RIV CE - Biochemistry R&D Projects GPP206/10/P018 GA ČR - Czech Science Foundation (CSF) GAP207/11/0455 GA ČR - Czech Science Foundation (CSF) GAP206/12/1150 GA ČR - Czech Science Foundation (CSF) ME10013 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GD204/09/H084 GA ČR - Czech Science Foundation (CSF) Institutional support MBU-M - RVO:61388971 ; FGU-C - RVO:67985823 UT WOS 000309396300004 DOI 10.1002/jms.3081 Annotation We report substantial in-situ enrichment of phosphopeptides in peptide mixtures using titanium and zirconium dioxide-coated matrix assisted laser desorption-ionization (MALDI) plates prepared by recently reported ambient ion landing deposition technique. The technique was able to modify four common materials currently used for MALDI targets (stainless steel, aluminum, indium-tin oxide glass and polymeric anchor chip). The structure of the deposited dioxide was investigated by electron microscopy, and different surfaces were compared and discussed in this study. Two standard proteins were used to test the enrichment capabilities of modified MALDI plates: casein and in-vitro phosphorylated trehalase. The enrichment of casein tryptic digest resulted in identification of 20 phosphopeptides (including miscleavages). Trehalase was used as a suitable model of larger protein that provided more complex peptide mixture after the trypsin digestion. All four possible phosphorylation sites in trehalase were identified and up to seven phosphopetides were found (including methionine oxidations and miscleavages). Two different mass spectrometers, MALDI-Fourier transform ion cyclotron resonance (FTICR) and MALDI-time of flight, were used to detect the phosphopeptides from modified MALDI plates after the enrichment procedure. It was observed that the desorption-ionization phenomena on the modified surfaces are not critically influenced by the parameters of the different MALDI ion sources (e.g. different pressure, different extraction voltages), and thus the presence of dioxide layer on the standard MALDI plate does not significantly interfere with the main MALDI processes Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2013
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