Laser post-ionisation combined with a high resolving power orbitrap mass spectrometer for enhanced MALDI-MS imaging of lipids

Coupling laser post-ionisation with a high resolving power MALDI Orbitrap mass spectrometer has realised an up to ∼100-fold increase in the sensitivity and enhanced the chemical coverage for MALDI-MS imaging of lipids relative to conventional MALDI.

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Subcellular-level resolution MALDI-MS imaging of maize leaf metabolites by MALDI-linear ion trap-Orbitrap mass spectrometer

Analytical and Bioanalytical Chemistry ◽

10.1007/s00216-015-8460-5 ◽

2015 ◽

Vol 407 (8) ◽

pp. 2301-2309 ◽

Cited By ~ 67

Author(s):

Andrew R. Korte ◽

Marna D. Yandeau-Nelson ◽

Basil J. Nikolau ◽

Young Jin Lee

Keyword(s):

Mass Spectrometer ◽

Ion Trap ◽

Maldi Ms ◽

Linear Ion Trap ◽

Maize Leaf ◽

Ms Imaging ◽

Orbitrap Mass Spectrometer ◽

Subcellular Level

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Limits for resolving tandem mass tag reporter ions with identical integer mass using phase constrained spectrum deconvolution

10.1101/332668 ◽

2018 ◽

Author(s):

Christian D. Kelstrup ◽

Konstantin Aizikov ◽

Tanveer S. Batth ◽

Arne Kreutzman ◽

Dmitry Grinfeld ◽

...

Keyword(s):

Mass Spectrometer ◽

Peptide Sequencing ◽

Mass Resolution ◽

Resolving Power ◽

Acquisition Time ◽

Tandem Mass ◽

Optimal Method ◽

Orbitrap Mass Spectrometer ◽

Mass Resolving Power ◽

Spectrum Deconvolution

ABSTRACTA popular method for peptide quantification relies on isobaric labeling such as tandem mass tags (TMT) which enables multiplexed proteome analyses. Quantification is achieved by reporter ions generated by fragmentation in a tandem mass spectrometer. However, with higher degrees of multiplexing, the smaller mass differences between the reporter ions increase the mass resolving power requirements. This contrasts with faster peptide sequencing capabilities enabled by lowered mass resolution on Orbitrap instruments. It is therefore important to determine the mass resolution limits for highly multiplexed quantification when maximizing proteome depth. Here we defined the lower boundaries for resolving TMT reporter ions with 0.0063 Da mass differences using an ultra-high-field Orbitrap mass spectrometer. We found the optimal method depends on the relative ratio between closely spaced reporter ions and that 64 ms transient acquisition time provided sufficient resolving power for separating TMT reporter ions with absolute ratio changes up to 16-fold. Furthermore, a 32 ms transient processed with phase-constrained spectrum deconvolution provides >50% more identifications with >99% quantified, but with a slight loss in quantification precision and accuracy. These findings should guide decisions on what Orbitrap resolution settings to use in future proteomics experiments relying on TMT reporter ion quantification with identical integer masses.

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Introduction of a 20 kHz Nd:YVO4 laser into a hybrid quadrupole time-of-flight mass spectrometer for MALDI-MS imaging

Analytical and Bioanalytical Chemistry ◽

10.1007/s00216-010-3874-6 ◽

2010 ◽

Vol 397 (8) ◽

pp. 3409-3419 ◽

Cited By ~ 65

Author(s):

Paul J. Trim ◽

Marie-Claude Djidja ◽

Sally J. Atkinson ◽

Keith Oakes ◽

Laura M. Cole ◽

...

Keyword(s):

Mass Spectrometer ◽

Time Of Flight ◽

Maldi Ms ◽

Flight Mass Spectrometer ◽

Ms Imaging

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Toward Revealing Microcystin Distribution in Mouse Liver Tissue Using MALDI-MS Imaging

Toxins ◽

10.3390/toxins13100709 ◽

2021 ◽

Vol 13 (10) ◽

pp. 709

Author(s):

Daria Kucheriavaia ◽

Dušan Veličković ◽

Nicholas Peraino ◽

Apurva Lad ◽

David J. Kennedy ◽

...

Keyword(s):

Mass Spectrometer ◽

Algal Blooms ◽

Maldi Ms ◽

High Mass ◽

Ionization Mass ◽

Ion Cyclotron Resonance ◽

Tissue Preparation ◽

Matrix Deposition ◽

Ms Imaging ◽

Ft Icr

Cyanotoxins can be found in water and air during cyanobacterial harmful algal blooms (cHABs) in lakes and rivers. Therefore, it is very important to monitor their potential uptake by animals and humans as well as their health effects and distribution in affected organs. Herein, the distribution of hepatotoxic peptide microcystin-LR (MC-LR) is investigated in liver tissues of mice gavaged with this most common MC congener. Preliminary matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) imaging experiments performed using a non-automated MALDI matrix deposition device and a MALDI-time-of-flight (TOF) mass spectrometer yielded ambiguous results in terms of MC-LR distribution in liver samples obtained from MC-LR-gavaged mice. The tissue preparation for MALDI-MS imaging was improved by using an automated sprayer for matrix deposition, and liver sections were imaged using an Nd:YAG MALDI laser coupled to a 15 Tesla Fourier-transform ion cyclotron resonance (FT-ICR)-mass spectrometer. MALDI-FT-ICR-MS imaging provided unambiguous detection of protonated MC-LR (calculated m/z 995.5560, z = +1) and the sodium adduct of MC-LR (m/z 1017.5380, z = +1) in liver sections from gavaged mice with great mass accuracy and ultra-high mass resolution. Since both covalently bound and free MC-LR can be found in liver of mice exposed to this toxin, the present results indicate that the distribution of free microcystins in tissue sections from affected organs, such as liver, can be monitored with high-resolution MALDI-MS imaging.

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