Approaching cellular resolution and reliable identification in mass spectrometry imaging of tryptic peptides

On-tissue digestion has become the preferred method to identify proteins in mass spectrometry (MS) imaging. In this study, we report advances in data acquisition and protein identification for MS imaging after on-tissue digestion. Tryptic peptides in a coronal mouse brain section were measured at 50...

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Bibliographic Details
Published in:Analytical and bioanalytical chemistry 2018-09, Vol.410 (23), p.5825-5837
Main Authors: Huber, Katharina, Khamehgir-Silz, Pegah, Schramm, Thorsten, Gorshkov, Vladimir, Spengler, Bernhard, Römpp, Andreas
Format: Article
Language:English
Subjects:
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Analytical Chemistry
Biochemistry
Brain
Cerebellum
Characterization and Evaluation of Materials
Chemistry
Chemistry and Materials Science
Data acquisition
Data processing
Digestion
Food Science
Identification
Imaging
Ions
Laboratory Medicine
Mass spectrometry
Mass spectroscopy
Methods
Monitoring/Environmental Analysis
Myelin
Neuroimaging
Peptides
Pixels
Properties
Proteins
Research Paper
Scientific imaging
Software development tools
Spatial discrimination
Spatial distribution
Spatial resolution
Spectroscopy
Staining
Tissues
Tryptic peptides
Workflow
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Summary:On-tissue digestion has become the preferred method to identify proteins in mass spectrometry (MS) imaging. In this study, we report advances in data acquisition and protein identification for MS imaging after on-tissue digestion. Tryptic peptides in a coronal mouse brain section were measured at 50 μm pixel size and revealed detailed histological structures, e.g., the ependyma (consisting of one to two cell layers), which was confirmed by H&E staining. This demonstrates that MS imaging of tryptic peptides at or close to cellular resolution is within reach. We also describe a detailed identification workflow which resulted in the identification of 99 proteins (with 435 corresponding peptides), based on comparison with LC-MS/MS data and in silico digest. These results were obtained with stringent parameters, including high mass accuracy in imaging mode (RSME
ISSN:1618-2642
1618-2650
DOI:10.1007/s00216-018-1199-z