TL;DR: Matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS) has been used to generate ion images of samples in one or more mass-to-charge (m/z) values, providing the capability of mapping specific molecules to two-dimensional coordinates of the original sample.
Abstract: Matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS) has been used to generate ion images of samples in one or more mass-to-charge (m/z) values, providing the capability of mapping specific molecules to two-dimensional coordinates of the original sample. The high sensitivity of the technique (low-femtomole to attomole levels for proteins and peptides) allows the study of organized biochemical processes occurring in, for example, mammalian tissue sections. The mass spectrometer is used to determine the molecular weights of the molecules in the surface layers of the tissue. Molecules desorbed from the sample typically are singly protonated, giving an ion at (M + H)+, where M is the molecular mass. The procedure involves coating the tissue section, or a blotted imprint of the section, with a thin layer of energy-absorbing matrix and then analyzing the sample to produce an ordered array of mass spectra, each containing nominal m/z values typically covering a range of over 50 000 Da. Images...
TL;DR: Imaging MS joins techniques such as immunochemistry and fluorescence microscopy for the study of the spatial arrangement of molecules within biological tissues for the unraveling and understanding the molecular complexities of cells.
Abstract: 1and has been initially targeted for the analysis of peptides and proteins present on or near the surface of tissue sections 2 . Imaging MS brings a new tool to bear on the problem of unraveling and understanding the molecular complexities of cells. It joins techniques such as immunochemistry and fluorescence microscopy for the study of the spatial arrangement of molecules within biological tissues. Many previous experiments using MS to image samples have focused on the measurement of the distribution of elements and small molecules in biological specimens, including tissue slices and individual cells 3‐5 . An extensive review on imaging by MS can be found in the article by Pacholski and Winograd 6
TL;DR: Many of the instrumental developments and methodological approaches responsible for an increasing upsurge in interest in imaging mass spectrometry are reviewed, compare and contrast the information provided by SIMS and MALDI imaging, and discuss future possibilities.
Abstract: Imaging mass spectrometry combines the chemical specificity and parallel detection of mass spectrometry with microscopic imaging capabilities. The ability to simultaneously obtain images from all analytes detected, from atomic to macromolecular ions, allows the analyst to probe the chemical organization of a sample and to correlate this with physical features. The sensitivity of the ionization step, sample preparation, the spatial resolution, and the speed of the technique are all important parameters that affect the type of information obtained. Recently, significant progress has been made in each of these steps for both secondary ion mass spectrometry (SIMS) and matrix-assisted laser desorption/ionization (MALDI) imaging of biological samples. Examples demonstrating localization of proteins in tumors, a reduction of lamellar phospholipids in the region binding two single celled organisms, and sub-cellular distributions of several biomolecules have all contributed to an increasing upsurge in interest in imaging mass spectrometry. Here we review many of the instrumental developments and methodological approaches responsible for this increased interest, compare and contrast the information provided by SIMS and MALDI imaging, and discuss future possibilities.
TL;DR: The current state of the art of MALDI-IMS is discussed along with some recent applications and technological developments that illustrate not only its current capabilities but also the future potential of the technique to provide a better understanding of the underlying molecular mechanisms of biological processes.
Abstract: Matrix-assisted laser desorption/ionization (MALDI) imaging mass spectrometry (IMS) is emerging as a powerful tool for investigating the distribution of molecules within biological systems through the direct analysis of thin tissue sections. Unique among imaging methods, MALDI-IMS can determine the distribution of hundreds of unknown compounds in a single measurement. We discuss the current state of the art of MALDI-IMS along with some recent applications and technological developments that illustrate not only its current capabilities but also the future potential of the technique to provide a better understanding of the underlying molecular mechanisms of biological processes.
TL;DR: A simple new sample preparation procedure in which matrix and sample handling are completely decoupled is described, which could be used for protein analysis in particular.
Abstract: Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI TOF) is becoming a standard tool in mass spectrometry in general and protein analysis in particular. Its advantage include high sensitivity, tolerance to buffers, fast data acquisition, and simple and robust instrumentation. Diadvantages have been caused by factors related to sample preparation. Here we describe a simple new sample preparation procedure in which matrix and sample handling are completely decoupled