Abstract：
:One of the important challenges for MALDI imaging mass spectrometry (MALDI-IMS) is the unambiguous identification of measured analytes. One way to do this is to match tryptic peptide MALDI-IMS m/z values with LC-MS/MS identified m/z values. Matching using current MALDI-TOF/TOF MS instruments is difficult due to the variability of in situ time-of-flight (TOF) m/z measurements. This variability is currently addressed using external calibration, which limits achievable mass accuracy for MALDI-IMS and makes it difficult to match these data to downstream LC-MS/MS results. To overcome this challenge, the work presented here details a method for internally calibrating data sets generated from tryptic peptide MALDI-IMS on formalin-fixed paraffin-embedded sections of ovarian cancer. By calibrating all spectra to internal peak features the m/z error for matches made between MALDI-IMS m/z values and LC-MS/MS identified peptide m/z values was significantly reduced. This improvement was confirmed by follow up matching of LC-MS/MS spectra to in situ MS/MS spectra from the same m/z peak features. The sum of the data presented here indicates that internal calibrants should be a standard component of tryptic peptide MALDI-IMS experiments.
journal_name
J Proteomicsjournal_title
Journal of proteomicsauthors
Gustafsson JOR,Eddes JS,Meding S,Koudelka T,Oehler MK,McColl SR,Hoffmann Pdoi
10.1016/j.jprot.2012.04.054subject
Has Abstractpub_date
2012-08-30 00:00:00pages
5093-5105issue
16eissn
1874-3919issn
1876-7737pii
S1874-3919(12)00325-9journal_volume
75pub_type
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