Protein identification strategies in MALDI imaging mass spectrometry: a brief review

[Display omitted] Matrix assisted laser desorption/ionization (MALDI) imaging mass spectrometry (IMS) is a powerful technology used to investigate the spatial distributions of thousands of molecules throughout a tissue section from a single experiment. As proteins represent an important group of fun...

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Vydané v:Current opinion in chemical biology Ročník 48; s. 64 - 72
Hlavní autori: Ryan, Daniel J, Spraggins, Jeffrey M, Caprioli, Richard M
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: England Elsevier Ltd 01.02.2019
Predmet:
Animals
Equipment Design
Humans
Molecular Imaging - instrumentation
Molecular Imaging - methods
Proteins - analysis
Proteins - isolation & purification
Specimen Handling - instrumentation
Specimen Handling - methods
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - instrumentation
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods
Workflow
ISSN:1367-5931, 1879-0402, 1879-0402
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Shrnutí:[Display omitted] Matrix assisted laser desorption/ionization (MALDI) imaging mass spectrometry (IMS) is a powerful technology used to investigate the spatial distributions of thousands of molecules throughout a tissue section from a single experiment. As proteins represent an important group of functional molecules in tissue and cells, the imaging of proteins has been an important point of focus in the development of IMS technologies and methods. Protein identification is crucial for the biological contextualization of molecular imaging data. However, gas-phase fragmentation efficiency of MALDI generated proteins presents significant challenges, making protein identification directly from tissue difficult. This review highlights methods and technologies specifically related to protein identification that have been developed to overcome these challenges in MALDI IMS experiments.
Bibliografia:ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:1367-5931
1879-0402
1879-0402
DOI:10.1016/j.cbpa.2018.10.023