Imaging mass spectrometry: principle and application #MMPMID28509996
Murayama C; Kimura Y; Setou M
Biophys Rev 2009[Sep]; 1 (3): ä PMID28509996show 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 MSn, 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.Electronic supplementary material: The online version of this article (doi:10.1007/s12551-009-0015-6) contains supplementary material, which is available to authorized users.
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Biophys+Rev 2009 ; 1 (3): ä
