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In-situ enrichment of phosphopeptides on MALDI plates modified by ambient ion landing.
MedLine Citation:
PMID:  23019160     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
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. The detection of phosphopeptides after the enrichment could be done by both instruments. Desorption electrospray ionization coupled to the FTICR was also tested, but, unlike MALDI, it did not provide satisfactory results. Copyright © 2012 John Wiley & Sons, Ltd.
Authors:
Lukáš Krásný; Petr Pompach; Martin Strohalm; Veronika Obsilova; Marcela Strnadová; Petr Novák; Michael Volný
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of mass spectrometry : JMS     Volume:  47     ISSN:  1096-9888     ISO Abbreviation:  J Mass Spectrom     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-09-28     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9504818     Medline TA:  J Mass Spectrom     Country:  England    
Other Details:
Languages:  eng     Pagination:  1294-302     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 John Wiley & Sons, Ltd.
Affiliation:
Institute of Microbiology of the ASCR, v.v.i., Videnska 1083, Prague 4, 142 20, Czech Republic; Institute of Chemical Technology, Technická 5, Prague, 16628, Czech Republic.
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