scholarly journals Spatial distribution of isobaric androgens in target tissues using chemical derivatization and MALDI-2 on a trapped ion mobility quadrupole time-of-flight instrument

RSC Advances ◽  
2021 ◽  
Vol 11 (54) ◽  
pp. 33916-33925
Author(s):  
C. L. Logan Mackay ◽  
Jens Soltwisch ◽  
Bram Heijs ◽  
Karl W. Smith ◽  
Faye L. Cruickshank ◽  
...  
Keyword(s):  
Spatial Distribution ◽  
Ion Mobility ◽  
Time Of Flight ◽  
Biological Tissues ◽  
Ionization Efficiency ◽  
Chemical Derivatization ◽  
Trapped Ion ◽  
Isobaric Separation ◽  
First Time

We increase ionization efficiency and isobaric separation of derivatized androgens using MALDI-2-TIMS. First time spatial distribution of isobaric androgens is achieved in biological tissues by on-tissue chemical derivatization and MALDI-2-TIMS-MSI.

scholarly journals High Performance Molecular Imaging with MALDI Trapped Ion Mobility Time-of-Flight (timsTOF) Mass Spectrometry

2019 ◽  
Author(s):  
Jeffrey Spraggins ◽  
Katerina Djambazova ◽  
Emilio Rivera ◽  
Lukasz Migas ◽  
Elizabeth Neumann ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Imaging ◽  
Spatial Resolution ◽  
Ion Mobility ◽  
Measurement Errors ◽  
High Performance ◽  
High Spatial Resolution ◽  
Biological Tissues ◽  
Whole Body ◽  
Trapped Ion

Imaging mass spectrometry (IMS) enables the spatially targeted molecular assessment of biological tissues at cellular resolutions. New developments and technologies are essential for uncovering the molecular drivers of native physiological function and disease. Instrumentation must maximize spatial resolution, throughput, sensitivity, and specificity, because tissue imaging experiments consist of thousands to millions of pixels. Here, we report the development and application of a matrix-assisted laser desorption/ionization (MALDI) trapped ion mobility spectrometry imaging platform. This prototype MALDI timsTOF instrument is capable of 10 µm spatial resolutions and 20 pixels/s throughput molecular imaging. The MALDI source utilizes a Bruker SmartBeam 3-D laser system that can generate a square burn pattern of <10 x 10 µm at the sample surface. General image performance was assessed using murine kidney and brain tissues and demonstrate that high spatial resolution imaging data can be generated rapidly with mass measurement errors < 5 ppm and ~40,000 resolving power. Initial TIMS-based imaging experiments were performed on whole body mouse pup tissue demonstrating the separation of closely isobaric [PC(32:0)+Na]<sup>+</sup>and [PC(34:3)+H]<sup>+</sup>(3 mDa mass difference) in the gas-phase. We have shown that the MALDI timsTOF platform can maintain reasonable data acquisition rates (>2 pixels/s) while providing the specificity necessary to differentiate components in complex mixtures of lipid adducts. The combination of high spatial resolution and throughput imaging capabilities with high-performance TIMS separations provides a uniquely tunable platform to address many challenges associated with advanced molecular imaging applications.

scholarly journals AlphaTims: Indexing trapped ion mobility spectrometry - time of flight data for fast and easy accession and visualization

2021 ◽  
Author(s):  
Sander Willems ◽  
Eugenia Voytik ◽  
Patricia Skowronek ◽  
Maximilian T Strauss ◽  
Matthias Mann
Keyword(s):  
Mass Spectrometry ◽  
Open Source ◽  
Ion Mobility Spectrometry ◽  
Ion Mobility ◽  
Large Scale ◽  
High Resolution Mass Spectrometry ◽  
Time Of Flight ◽  
Arrival Times ◽  
Trapped Ion ◽  
Trapped Ion Mobility Spectrometry

High resolution mass spectrometry-based proteomics generates large amounts of data, even in the standard liquid chromatography (LC) - tandem mass spectrometry configuration. Adding an ion mobility dimension vastly increases the acquired data volume, challenging both analytical processing pipelines and especially data exploration by scientists. This has necessitated data aggregation, effectively discarding much of the information present in these rich data sets. Taking trapped ion mobility spectrometry (TIMS) on a quadrupole time-of-flight platform (Q-TOF) as an example, we developed an efficient indexing scheme that represents all data points as detector arrival times on scales of minutes (LC), milliseconds (TIMS) and microseconds (TOF). In our open source AlphaTims package, data are indexed, accessed and visualized by a combination of tools of the scientific Python ecosystem. We interpret unprocessed data as a sparse 4D matrix and use just-in-time compilation to machine code with Numba, accelerating our computational procedures by several orders of magnitude while keeping to familiar indexing and slicing notations. For samples with more than six billion detector events, a modern laptop can load and index raw data in about a minute. Loading is even faster when AlphaTims has already saved indexed data in a HDF5 file, a portable scientific standard used in extremely large-scale data acquisition. Subsequently, data accession along any dimension and interactive visualization happen in milliseconds. We have found AlphaTims to be a key enabling tool to explore high dimensional LC-TIMS-QTOF data and have made it freely available as an open-source Python package with a stand-alone graphical user interface at https://github.com/MannLabs/alphatims or as part of the AlphaPept ecosystem.

High Performance Molecular Imaging with MALDI Trapped Ion Mobility Time-of-Flight (timsTOF) Mass Spectrometry

2019 ◽  
Author(s):  
Jeffrey Spraggins ◽  
Katerina Djambazova ◽  
Emilio Rivera ◽  
Lukasz Migas ◽  
Elizabeth Neumann ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Imaging ◽  
Spatial Resolution ◽  
Ion Mobility ◽  
Measurement Errors ◽  
High Performance ◽  
High Spatial Resolution ◽  
Biological Tissues ◽  
Whole Body ◽  
Trapped Ion

Imaging mass spectrometry (IMS) enables the spatially targeted molecular assessment of biological tissues at cellular resolutions. New developments and technologies are essential for uncovering the molecular drivers of native physiological function and disease. Instrumentation must maximize spatial resolution, throughput, sensitivity, and specificity, because tissue imaging experiments consist of thousands to millions of pixels. Here, we report the development and application of a matrix-assisted laser desorption/ionization (MALDI) trapped ion mobility spectrometry imaging platform. This prototype MALDI timsTOF instrument is capable of 10 µm spatial resolutions and 20 pixels/s throughput molecular imaging. The MALDI source utilizes a Bruker SmartBeam 3-D laser system that can generate a square burn pattern of <10 x 10 µm at the sample surface. General image performance was assessed using murine kidney and brain tissues and demonstrate that high spatial resolution imaging data can be generated rapidly with mass measurement errors < 5 ppm and ~40,000 resolving power. Initial TIMS-based imaging experiments were performed on whole body mouse pup tissue demonstrating the separation of closely isobaric [PC(32:0)+Na]<sup>+</sup>and [PC(34:3)+H]<sup>+</sup>(3 mDa mass difference) in the gas-phase. We have shown that the MALDI timsTOF platform can maintain reasonable data acquisition rates (>2 pixels/s) while providing the specificity necessary to differentiate components in complex mixtures of lipid adducts. The combination of high spatial resolution and throughput imaging capabilities with high-performance TIMS separations provides a uniquely tunable platform to address many challenges associated with advanced molecular imaging applications.

High Performance Molecular Imaging with MALDI Trapped Ion Mobility Time-of-Flight (timsTOF) Mass Spectrometry

2019 ◽  
Author(s):  
Jeffrey Spraggins ◽  
Katerina Djambazova ◽  
Emilio Rivera ◽  
Lukasz Migas ◽  
Elizabeth Neumann ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Imaging ◽  
Spatial Resolution ◽  
Ion Mobility ◽  
Measurement Errors ◽  
High Performance ◽  
High Spatial Resolution ◽  
Biological Tissues ◽  
Whole Body ◽  
Trapped Ion

Imaging mass spectrometry (IMS) enables the spatially targeted molecular assessment of biological tissues at cellular resolutions. New developments and technologies are essential for uncovering the molecular drivers of native physiological function and disease. Instrumentation must maximize spatial resolution, throughput, sensitivity, and specificity, because tissue imaging experiments consist of thousands to millions of pixels. Here, we report the development and application of a matrix-assisted laser desorption/ionization (MALDI) trapped ion mobility spectrometry imaging platform. This prototype MALDI timsTOF instrument is capable of 10 µm spatial resolutions and 20 pixels/s throughput molecular imaging. The MALDI source utilizes a Bruker SmartBeam 3-D laser system that can generate a square burn pattern of <10 x 10 µm at the sample surface. General image performance was assessed using murine kidney and brain tissues and demonstrate that high spatial resolution imaging data can be generated rapidly with mass measurement errors < 5 ppm and ~40,000 resolving power. Initial TIMS-based imaging experiments were performed on whole body mouse pup tissue demonstrating the separation of closely isobaric [PC(32:0)+Na]<sup>+</sup>and [PC(34:3)+H]<sup>+</sup>(3 mDa mass difference) in the gas-phase. We have shown that the MALDI timsTOF platform can maintain reasonable data acquisition rates (>2 pixels/s) while providing the specificity necessary to differentiate components in complex mixtures of lipid adducts. The combination of high spatial resolution and throughput imaging capabilities with high-performance TIMS separations provides a uniquely tunable platform to address many challenges associated with advanced molecular imaging applications.

scholarly journals Exploration of human cerebrospinal fluid: A large proteome dataset revealed by trapped ion mobility time-of-flight mass spectrometry

Data in Brief ◽  
2020 ◽  
Vol 31 ◽  
pp. 105704 ◽  
Author(s):  
Charlotte Macron ◽  
Regis Lavigne ◽  
Antonio Núñez Galindo ◽  
Michael Affolter ◽  
Charles Pineau ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Cerebrospinal Fluid ◽  
Ion Mobility ◽  
Time Of Flight ◽  
Trapped Ion ◽  
Flight Mass Spectrometry ◽  
Human Cerebrospinal Fluid

scholarly journals Investigation of tear protein composition in healthy and dry eye subjects using trapped ion mobility spectrometry coupled with quadrupole time of flight

2019 ◽  
Vol 97 (S263) ◽  
Author(s):  
Ioannis Kolman ◽  
Karima Kessal ◽  
Solenne Chardonnet ◽  
Stéphane Mélik Parsadaniantz ◽  
Christophe Baudouin ◽  
...  
Keyword(s):  
Dry Eye ◽  
Ion Mobility Spectrometry ◽  
Ion Mobility ◽  
Time Of Flight ◽  
Protein Composition ◽  
Trapped Ion ◽  
Tear Protein ◽  
Trapped Ion Mobility Spectrometry
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