Use of advantageous, volatile matrices enabled by next-generation high-speed matrix-assisted laser desorption/ionization time-of-flight imaging employing a scanning laser beam

Ogrinc, Nina; Porta, Tiffany; Becker, Michael; Heeren, Ron M. A.; Ellis, Shane R.

doi:10.1002/rcm.7379

Cited by 124 publications

(108 citation statements)

References 27 publications

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“…At present, IMS could be considered as a complementary method that may give valuable information during preclinical studies of drug candidates as well as in toxicological research. As the work with technical improvements is continuously ongoing, IMS could be expected to become a standard method in drug development and toxicology (Fisher et al 2016; Ogrinc Potocnik et al 2015; Prentice et al 2016). …”

Section: Discussionmentioning

confidence: 99%

Imaging mass spectrometry in drug development and toxicology

2016

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During the last decades, imaging mass spectrometry has gained significant relevance in biomedical research. Recent advances in imaging mass spectrometry have paved the way for in situ studies on drug development, metabolism and toxicology. In contrast to whole-body autoradiography that images the localization of radiolabeled compounds, imaging mass spectrometry provides the possibility to simultaneously determine the discrete tissue distribution of the parent compound and its metabolites. In addition, imaging mass spectrometry features high molecular specificity and allows comprehensive, multiplexed detection and localization of hundreds of proteins, peptides and lipids directly in tissues. Toxicologists traditionally screen for adverse findings by histopathological examination. However, studies of the molecular and cellular processes underpinning toxicological and pathologic findings induced by candidate drugs or toxins are important to reach a mechanistic understanding and an effective risk assessment strategy. One of IMS strengths is the ability to directly overlay the molecular information from the mass spectrometric analysis with the tissue section and allow correlative comparisons of molecular and histologic information. Imaging mass spectrometry could therefore be a powerful tool for omics profiling of pharmacological/toxicological effects of drug candidates and toxicants in discrete tissue regions. The aim of the present review is to provide an overview of imaging mass spectrometry, with particular focus on MALDI imaging mass spectrometry, and its use in drug development and toxicology in general.

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Section: Discussionmentioning

confidence: 99%

Imaging mass spectrometry in drug development and toxicology

2016

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“…The recent development of high lateral resolution commercial MALDI MSI mass spectrometers with 5 μm laser spot size points to high-resolution MSI of large biomolecules in tissue becoming routine [18, 62]. Even with a small laser spot size, there remain challenges for biomolecule imaging in developing protocols for matrix addition without sample migration, achieving adequate sensitivity for large molecules at small laser spot sizes [4], and developing methods for compound identification and quantification [122, 123].…”

Section: Discussionmentioning

confidence: 99%

“…The resolution of MALDI MSI is influenced by the same factors as laser microprobe MSI with the additional constraint that a matrix must be added, which can result in the migration of biomolecules in tissue samples [8, 61]. The lateral resolution of commercial MALDI MSI instruments has remained in this range in the intervening years, although there is a recent move to bring imaging below the 10 μm range for routine analysis [18, 62]. Imaging at atmospheric pressure is also moving to the sub-10 μm regime [63].…”

Section: Maldi Msimentioning

confidence: 99%

“…Imaging at atmospheric pressure is also moving to the sub-10 μm regime [63]. Another notable if more incremental improvement in MALDI MSI has been the steady increase in data acquisition speed, which has increased due to improvements in signal digitization electronics and the replacement of relatively low-repetition rate 337 nm nitrogen lasers with frequency-tripled 355 nm Nd:YAG lasers with repetition rates up to 10 kHz [18] and 349 nm Nd:YLF lasers with a repetition rate of 5 kHz [64]. …”

Section: Maldi Msimentioning

confidence: 99%

“…The mass range of laser-based MSI was significantly extended with the application of matrix-assisted laser desorption/ionization (MALDI) by Caprioli and coworkers in the late 1990s [17]. With current instrumentation, MALDI MSI has a working mass range up to 30 kDa [8]; the lateral resolution has improved from approximately 50 μm to the point where the latest commercial instruments are approaching 10 μm resolution [18]. …”

Section: Introductionmentioning

confidence: 99%

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High resolution laser mass spectrometry bioimaging

Murray

Seneviratne

Ghorai

2016

Methods

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MSI (MSI) was introduced more than five decades ago with secondary ion mass spectrometry (SIMS) and a decade later with laser desorption/ionization (LDI) mass spectrometry (MS). Large biomolecule imaging by matrix-assisted laser desorption/ionization (MALDI) was developed in the 1990s and ambient laser MS a decade ago. Although SIMS has been capable of imaging with a moderate mass range at sub-micrometer lateral resolution from its inception, laser MS requires additional effort to achieve a lateral resolution of 10 μm or below which is required to image at the size scale of single mammalian cells. This review covers untargeted large biomolecule MSI using lasers for desorption/ionization or laser desorption and post-ionization. These methods include laser microprobe (LDI) MSI, MALDI MSI, laser ambient and atmospheric pressure MSI, and near-field laser ablation MS. Novel approaches to improving lateral resolution are discussed, including oversampling, beam shaping, transmission geometry, reflective and through-hole objectives, microscope mode, and near-field optics.

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The journey towards clinical adoption of MALDI‐MS‐based imaging proteomics: from current challenges to future expectations

Piga,

Magni,

Smith

2024

FEBS Letters

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Among the spatial omics techniques available, mass spectrometry imaging (MSI) represents one of the most promising owing to its capability to map the distribution of hundreds of peptides and proteins, as well as other classes of biomolecules, within a complex sample background in a multiplexed and relatively high‐throughput manner. In particular, matrix‐assisted laser desorption/ionisation (MALDI‐MSI) has come to the fore and established itself as the most widely used technique in clinical research. However, the march of this technique towards clinical utility has been hindered by issues related to method reproducibility, appropriate biocomputational tools, and data storage. Notwithstanding these challenges, significant progress has been achieved in recent years regarding multiple facets of the technology and has rendered it more suitable for a possible clinical role. As such, there is now more robust and extensive evidence to suggest that the technology has the potential to support clinical decision‐making processes under appropriate circumstances. In this review, we will discuss some of the recent developments that have facilitated this progress and outline some of the more promising clinical proteomics applications which have been developed with a clear goal towards implementation in mind.

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Use of advantageous, volatile matrices enabled by next-generation high-speed matrix-assisted laser desorption/ionization time-of-flight imaging employing a scanning laser beam

Cited by 124 publications

References 27 publications

Imaging mass spectrometry in drug development and toxicology

Imaging mass spectrometry in drug development and toxicology

High resolution laser mass spectrometry bioimaging

The journey towards clinical adoption of MALDI‐MS‐based imaging proteomics: from current challenges to future expectations

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