MALDI MS Imaging at Acquisition Rates Exceeding 100 Pixels per Second

Bednařík, Antonín; Machálková, Markéta; Moskovets, Eugene; Coufalíková, Kateřina; Krásenský, Pavel; Houška, Pavel; Kroupa, Jiří; Navrátilová, Jarmila; Šmarda, Jan; Preisler, Jan

doi:10.1007/s13361-018-2078-8

Cited by 26 publications

(26 citation statements)

References 42 publications

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“…MSI is becoming a powerful analytical tool in biomedical and life sciences . The instrument technologies of MALDI mass spectrometers have greatly advanced in the past decade: for instance, implementing high‐repetition solid‐state lasers, continuous raster sampling, and galvanometer‐based optical scanners for improved throughput; spatially structured laser beam profiles and laser‐induced post‐ionization for improved sensitivity; laser beam shaping, fiber‐optic laser delivery systems, and transmission geometry vacuum MALDI source for improved spatial resolution; stigmatic imaging (microscope mode) instrumentation for both throughput and spatial resolution; and most recently, high‐performance elevated/atmospheric pressure MALDI . It could be argued that MALDI‐MSI applications have led this progress.…”

Section: Introductionmentioning

confidence: 99%

DIUTHAME enables matrix‐free mass spectrometry imaging of frozen tissue sections

Kuwata

Itou

Kotani

et al. 2020

Rapid Comm Mass Spectrometry

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Rationale:A recently developed matrix-free laser desorption/ionization method, DIUTHAME (desorption ionization using through-hole alumina membrane), was examined for the feasibility of mass spectrometry imaging (MSI) applied to frozen tissue sections. The permeation behavior of DIUTHAME is potentially useful for MSI as positional information may not be distorted during the extraction of analytes from a sample. Methods:The through-hole porous alumina membranes used in the DIUTHAME chips were fabricated by wet anodization, were 5 μm thick, and had the desired values of 200 nm through-hole diameter and 50% open aperture ratio. Mouse brain frozen tissue sections on indium tin oxide (ITO)-coated slides were covered using the DIUTHAME chips and were subjected to MSI experiments in commercial time-offlight mass spectrometers equipped with solid-state UV lasers after thawing and drying without matrix application.Result: Mass spectra and mass images were successfully obtained from the frozen tissue sections using DIUTHAME as the ionization method. The mass spectra contained rich peaks in the phospholipid mass range free from the chemical background owing to there being no matrix-derived peaks in that range. DIUTHAME-MSI delivered high-quality mass images that reflected the anatomy of the brain tissue. Conclusions:Analytes can be extracted from frozen tissue by capillary action of the through-holes in DIUTHAME and moisture contained in the tissue without distorting positional information of the analytes. The sample preparation for frozen tissue sections in DIUTHAME-MSI is simple, requiring no specialized skills or dedicated apparatus for matrix application. DIUTHAME can facilitate MSI at a low mass, as there is no interference from matrix-derived peaks, and should provide high-quality, reproducible mass images more easily than MALDI-MSI.

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Section: Introductionmentioning

confidence: 99%

DIUTHAME enables matrix‐free mass spectrometry imaging of frozen tissue sections

Kuwata

Itou

Kotani

et al. 2020

Rapid Comm Mass Spectrometry

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“…There are considerable advantages to LAST compared to direct MS imaging techniques such as MALDI 15,[17][18][19]65 or DESI, 21 despite LAST's lower lateral resolution. The delocalization introduced by the matrix 66 or the solvent spray 67 and the less efficient desorption of large biomolecules 68 in direct MS imaging methods are eliminated using LAST.…”

Section: Discussionmentioning

confidence: 99%

“…16,17 Improvements in spatial resolution and sensitivity in MALDI-MS imaging have been achieved using high mass resolution/accuracy MS instrumentation, methodologies to spray thin and even coatings of the matrix, new matrices, and better laser spot focusing. 15,[17][18][19] Another popular method in MS imaging crosses the ablation plume formed by a mid-infrared ns laser pulse with the output from an electrospray ionization source (sometimes referred to as laser ablation electrospray ionization or LAESI). 20 Laser wavelengths near ~3 µm are resonant with the OH stretch vibrations of water, facilitating explosive plume-like ablation from biofilms and other hydrated biological samples.…”

Section: Introductionmentioning

confidence: 99%

Spatially resolved analysis ofPseudomonas aeruginosabiofilm proteomes measured by laser ablation sample transfer

Pulukkody

Yung

Donnarumma

et al. 2021

Preprint

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Heterogeneity in the distribution of nutrients and O 2 gradients during biofilm growth gives rise to changes in phenotype. There has been long term interest in identifying spatial differences during biofilm development including clues that identify chemical heterogeneity. Laser ablation sample transfer (LAST) allows site-specific sampling combined with label free proteomics to distinguish radially and axially resolved proteomes for Pseudomonas aeruginosa biofilms. Specifically, differential protein abundances on oxic vs. anoxic regions of a biofilm was observed by combining LAST with bottom up proteomics. This study reveals active metabolism in the anoxic region of the biofilm with respect to the oxic region in P. aeruginosa , an aerobe by nature. Protein abundance data related to cellular acclimations to chemical gradients include identification of glucose catabolizing proteins, high abundance of proteins from arginine and polyamine metabolism, and proteins that could also support virulence and environmental stress mediation on the anoxic region. Finally, this methodology requires only a few mm 2 of biofilm area to identify hundreds of proteins.

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“…When the crystals are irradiated with the pulsed laser light of the MALDI source, the laser energy is absorbed by the matrix molecules and facilitate the explosive desorption and ionization. 1) Commercial MALDI MSI instruments allow acquisition rates up to 50 pixels/second and spatial resolutions down to 10 µm, 10) while experimental instruments are approaching 147 pixels/seconds, 11) or a spatial resolution of 1.4 µm. 12)…”

Section: Surface Sampling and Ionizationmentioning

confidence: 99%

Imaging Isomers on a Biological Surface: A Review

et al. 2019

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Mass spectrometry imaging is an imaging technology that allows the localization and identi cation of molecules on (biological) sample surfaces. Obtaining the localization of a compound in tissue is of great value in biological research. Yet, the identi cation of compounds remains a challenge. Mass spectrometry alone, even with high-mass resolution, cannot always distinguish between the subtle structural di erences of isomeric compounds. is review discusses recent advances in mass spectrometry imaging of lipids, steroid hormones, amino acids and proteins that allow imaging with isomeric resolution. ese improvements in detailed identi cation can give new insights into the local biological activity of isomers.

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MALDI MS Imaging at Acquisition Rates Exceeding 100 Pixels per Second

Cited by 26 publications

References 42 publications

DIUTHAME enables matrix‐free mass spectrometry imaging of frozen tissue sections

DIUTHAME enables matrix‐free mass spectrometry imaging of frozen tissue sections

Spatially resolved analysis ofPseudomonas aeruginosabiofilm proteomes measured by laser ablation sample transfer

Imaging Isomers on a Biological Surface: A Review

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