Abstract

Matrix-assisted laser desorption/ionization (MALDI) imaging mass spectrometry (IMS) is a technique that localizes the spatial distribution of molecules and identifies structures by their molecular mass signatures. Recently, the resolution of MALDI-IMS has been up to microscopic level. MALDI-IMS does not need either separation or purification procedures of target molecules and enables us to observe the localization of numerous molecules simultaneously. In particular, MALDI-MS time-of-flight/time-of-flight (TOF/TOF) is one of the instruments widely adopted for IMS, which allows the analysis of numerous biomolecules ranging over wide molecular weights. Even in a single data point, hundreds and thousands of mass peaks can be detected, and this makes the resulting mass spectrum extremely complex. This enormous volume of IMS data has driven the development of statistical approaches, especially multivariate analyses. By employing these approaches, researchers can figure out the important characteristics of their IMS data sets. The establishment of automatic molecular identification procedures involving MS(2) analysis, also known as MS/MS, performed by tandem mass spectrometry to obtain the information about molecular structure and composition, and database search available on the web is an important task for the near future. In this review, we introduce IMS-especially MALDI-IMS-with reference to its applications in biomolecular analyses, the workflow of IMS, the principle of IMS and other related technologies.

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