Proteome Imaging: From Classic to Modern Mass Spectrometry-Based Molecular Histology

Neagu, Anca-Narcisa

doi:10.1007/978-3-030-15950-4_4

Cited by 10 publications

(5 citation statements)

References 396 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Mass spectrometry imaging (MSI) is an emerging technology with substantial potential in biomedicine, including advancements in biomarker discovery, metabolomics studies, drug applications, and clinical diagnostics [ 195 , 196 ]. Considerable achievements have been realized in using MSI to visualize the distribution of AMPs in tissues and cells.…”

Section: Application Of Ms In Amps Studymentioning

confidence: 99%

Applications of tandem mass spectrometry (MS/MS) in antimicrobial peptides field: Current state and new applications

Fang,

Yu,

et al. 2024

Heliyon

View full text Add to dashboard Cite

Section: Application Of Ms In Amps Studymentioning

confidence: 99%

Applications of tandem mass spectrometry (MS/MS) in antimicrobial peptides field: Current state and new applications

Fang,

Yu,

et al. 2024

Heliyon

View full text Add to dashboard Cite

“…In recent years, this aspect has been rapidly progressing with the development of instruments equipped with low-diameter laser beams, suitable for high spatial resolution imaging. , There is no doubt that the ability to resolve the spatial localization of multiple proteins within a single section of pathological tissue can enable the detection of disease candidates and improve our understanding of pathophysiology. Nevertheless, the method still requires extensive tissue preparation techniques . Tissues must be pretreated with a matrix, and although multiple matrix options and coating methods are available, the commonly used matrices are acidic and contain organic solvents, which tend to denature the proteins of interest. , Thus, while intact proteins can be ionized in the presence of detergents and high salt concentrations, the preservation of protein–protein or protein–ligand interactions is challenging. , …”

Section: Maldi Imaging Msmentioning

confidence: 99%

Mass Spectrometry Analysis of Intact Proteins from Crude Samples

2020

View full text Add to dashboard Cite

Analysis of intact proteins by native mass spectrometry has emerged as a powerful tool for obtaining insight into subunit diversity, post-translational modifications, stoichiometry, structural arrangement, stability, and overall architecture. Typically, such an analysis is performed following protein purification procedures, which are time consuming, costly, and labor intensive. As this technology continues to move forward, advances in sample handling and instrumentation have enabled the investigation of intact proteins in situ and in crude samples, offering rapid analysis and improved conservation of the biological context. This emerging field, which involves various ion source platforms such as matrix-assisted laser desorption ionization (MALDI) and electrospray ionization (ESI) for both spatial imaging and solution-based analysis, is expected to impact many scientific fields, including biotechnology, pharmaceuticals, and clinical sciences. In this Perspective, we discuss the information that can be retrieved by such experiments as well as the current advantages and technical challenges associated with the different sampling strategies. Furthermore, we present future directions of these MS-based methods, including current limitations and efforts that should be made to make these approaches more accessible. Considering the vast progress we have witnessed in recent years, we anticipate that the advent of further innovations enabling minimal handling of MS samples will make this field more robust, user friendly, and widespread.

show abstract

“…Analysis of the spatial distribution of biomolecules in tissue is an important aspect of life sciences research and involves a wide range of techniques. − Mass spectrometry imaging (MSI) is routinely used to map the spatial distribution of metals and small molecules (e.g., metabolites and lipids , ) with a variety of different sampling techniques. MSI of intact proteins is much less common due to the technical challenges of ionizing proteins directly from a substrate and manipulating large ions in the gas phase.…”

Section: Introductionmentioning

confidence: 99%

High-Throughput Deconvolution of Native Protein Mass Spectrometry Imaging Data Sets for Mass Domain Analysis

Hale,

Cooper,

Marty

2023

Anal. Chem.

View full text Add to dashboard Cite

Protein mass spectrometry imaging (MSI) with electrospray-based ambient ionization techniques, such as nanospray desorption electrospray ionization (nano-DESI), generates data sets in which each pixel corresponds to a mass spectrum populated by peaks corresponding to multiply charged protein ions. Importantly, the signal associated with each protein is split among multiple charge states. These peaks can be transformed into the mass domain by spectral deconvolution. When proteins are imaged under native/non-denaturing conditions to retain non-covalent interactions, deconvolution is particularly valuable in helping interpret the data. To improve the acquisition speed, signal-to-noise ratio, and sensitivity, native MSI is usually performed using mass resolving powers that do not provide isotopic resolution, and conventional algorithms for deconvolution of lower-resolution data are not suitable for these large data sets. UniDec was originally developed to enable rapid deconvolution of complex protein mass spectra. Here, we developed an updated feature set harnessing the high-throughput module, MetaUniDec, to deconvolve each pixel of native MSI data sets and transform m/z-domain image files to the mass domain. New tools enable the reading, processing, and output of open format .imzML files for downstream analysis. Transformation of data into the mass domain also provides greater accessibility, with mass information readily interpretable by users of established protein biology tools such as sodium dodecyl sulfate polyacrylamide gel electrophoresis.

show abstract

Proteome Imaging: From Classic to Modern Mass Spectrometry-Based Molecular Histology

Cited by 10 publications

References 396 publications

Applications of tandem mass spectrometry (MS/MS) in antimicrobial peptides field: Current state and new applications

Applications of tandem mass spectrometry (MS/MS) in antimicrobial peptides field: Current state and new applications

Mass Spectrometry Analysis of Intact Proteins from Crude Samples

High-Throughput Deconvolution of Native Protein Mass Spectrometry Imaging Data Sets for Mass Domain Analysis

Contact Info

Product

Resources

About