Matrix-assisted Laser Desorption Ionization
Matrix-assisted Laser Desorption Ionization - Related Videos
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Matrix-Assisted Laser Desorption Ionization (MALDI)
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2025
Matrix-assisted laser desorption ionization (MALDI) is a powerful analytical technique used in mass spectrometry. It enables the identification and characterization of various biomolecules, including proteins, peptides, nucleic acids, and carbohydrates. MALDI is an ionization technique, widely employed in biological and medical research, as well as in fields like pharmacology and biochemistry.The analyte of interest, a biomolecule or a mixture of biomolecules, is mixed with a suitable matrix...
09:38
Dithranol as a Matrix for Matrix Assisted Laser Desorption/Ionization Imaging on a Fourier Transform Ion Cyclotron Resonance Mass Spectrometer
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Cited by 3 •
2013
Dithranol (DT; 1,8-dihydroxy-9,10-dihydroanthracen-9-one) has previously been reported as a MALDI matrix for tissue imaging of small molecules; protocols for the use of DT for the MALDI imaging of endogenous lipids on the surface of tissue sections by positive-ion MALDI-MS on an ultrahigh-resolution quadrupole-FTICR instrument are provided here.
10:47
Whole-body Mass Spectrometry Imaging by Infrared Matrix-assisted Laser Desorption Electrospray Ionization (IR-MALDESI)
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Cited by 19 •
2016
A mass spectrometry imaging (MSI) source operated at atmospheric pressure was developed by coupling mid-infrared laser desorption and electrospray post-ionization. Exogenous ice matrix was used as the energy-absorbing matrix to facilitate resonant desorption of tissue-related material. This manuscript provides a step-by-step protocol for performing IR-MALDESI MSI of whole-body neonatal mouse.
08:51
Profiling of Permethylated Mucin O-glycans Using Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry
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2025
Here, we present a detailed protocol for the release of O-glycans from mucins, and the subsequent desalting, permethylation, and analysis using MALDI-TOF mass spectrometry.
07:49
Matrix-assisted Laser Desorption/Ionization Time of Flight (MALDI-TOF) Mass Spectrometric Analysis of Intact Proteins Larger than 100 kDa
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Cited by 63 •
2013
Accurate mass measurement represents an important step during the investigation of proteins. Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) can be used for such determination and its key advantage is the tolerance to salts, detergents and contaminants. Here we illustrate an accessible approach for the analysis of proteins larger than 100 kDa by MALDI-MS.
FAQs
The matrix is a light-absorbing material that shares the dried sample spot with the analyte. After laser exposure, it absorbs the laser energy and promotes the analyte’s transfer into the gas phase and ion formation. This energy-transfer arrangement supports analysis of biological molecules such as peptides, proteins, lipids, and nucleic acids.
The crystalline spot places matrix and analyte together before irradiation. This arrangement allows the light-absorbing matrix to interact with the laser and promote desorption and ionization of the sample. Consequently, the prepared spot is the form in which MALDI handles biological analytes for subsequent mass-to-charge analysis.
Once MALDI generates gas-phase ions, the mass spectrometer separates them according to their mass-to-charge ratios. Time-of-flight analysis is one common way to perform that separation, allowing the resulting signal to be associated with different molecular masses relative to charge. In biological studies, this supports identification and measurement rather than merely detecting a laser response.
The preparation workflow begins by combining the biological sample with a light-absorbing matrix. The mixture is then dried into a crystalline spot before laser exposure. This sequence is important because the matrix must be present with the analyte when energy is delivered, enabling the later generation of ions for mass-to-charge separation.
MALDI supports several complementary biological uses. In biomarker research, it can contribute to identifying and measuring molecular signals; in microbial identification, it helps support identification of biological samples. Proteomics extends the approach to protein-focused studies, while spatial molecular imaging applies it to tissue sections. These use cases show why the technique is relevant across biology.
For tissue sections, MALDI can analyze molecules directly within the tissue rather than requiring the material to be considered only as a separate prepared mixture. This spatial capability makes the technique useful for molecular imaging, where measurements retain information about molecular location. It therefore connects biological molecule analysis with tissue organization.