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Phosphopeptide enrichment with stable spatial coordination on a titanium dioxide coated glass slide
Author(s) -
Imanishi Susumu Y.,
Kouvonen Petri,
Smått JanHenrik,
Heikkilä Mikko,
Peuhu Emilia,
Mikhailov Andrey,
Ritala Mikko,
Lindén Mika,
Corthals Garry L.,
Eriksson John E.
Publication year - 2009
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.4291
Subject(s) - phosphopeptide , chemistry , phosphoproteomics , mass spectrometry , phosphorylation , titanium dioxide , chromatography , mass spectrometry imaging , nanotechnology , protein phosphorylation , biochemistry , chemical engineering , protein kinase a , materials science , engineering
Recent advances in phosphoproteomics have established powerful tools to analyze phosphorylation events. However, their spatial localization is lost due to sample homogenization procedures prior to the analysis. Imaging mass spectrometry (IMS) has emerged as a method to visualize the spatial distribution of molecules in tissue samples, but its application is still limited to relatively abundant molecules. Due to low phosphorylation stoichiometry, direct detection and imaging of protein phosphorylation by MS has not been achieved yet. Therefore we have developed a novel phosphopeptide enrichment strategy as a potential tool for in situ affinity imaging MS (AIMS). A specific type of titanium dioxide (TiO 2 )‐coated glass slides was designed and validated with casein tryptic digests for their ability to selectively retain phosphopeptides while maintaining their spatial coordination. Copyright © 2009 John Wiley & Sons, Ltd.