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2009 ; 1
(3
): 131
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Imaging mass spectrometry: principle and application
#MMPMID28509996
Murayama C
; Kimura Y
; Setou M
Biophys Rev
2009[Sep]; 1
(3
): 131
PMID28509996
show ga
Imaging mass spectrometry (IMS) is two-dimensional mass spectrometry to visualize
the spatial distribution of biomolecules, which does not need either separation
or purification of target molecules, and enables us to monitor not only the
identification of unknown molecules but also the localization of numerous
molecules simultaneously. Among the ionization techniques, matrix assisted laser
desorption/ionization (MALDI) is one of the most generally used for IMS, which
allows the analysis of numerous biomolecules ranging over wide molecular weights.
Proper selection and preparation of matrix is essential for successful imaging
using IMS. Tandem mass spectrometry, which is referred to MS(n), enables the
structural analysis of a molecule detected by the first step of IMS. Applications
of IMS were initially developed for studying proteins or peptides. At present,
however, targets of IMS research have expanded to the imaging of small endogenous
metabolites such as lipids, exogenous drug pharmacokinetics, exploring new
disease markers, and other new scientific fields. We hope that this new
technology will open a new era for biophysics.
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