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Imaging Capabilities of a Low-Cost Benchtop MALDI-TOF Mass Spectrometer

Posters | 2021 | Shimadzu | ASMSInstrumentation
MALDI, LC/TOF, LC/MS
Industries
Clinical Research
Manufacturer
Shimadzu

Summary

Significance of the Topic


Matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI-MSI) enables spatial mapping of biomolecules in tissues, offering insights into molecular distributions underlying physiological and pathological processes. The adaptation of this technique to a low-cost benchtop MALDI-TOF instrument broadens accessibility, supporting applications in research, quality control, and education.

Objectives and Study Overview


This study assesses the imaging performance of a Shimadzu MALDI-8020 benchtop linear TOF mass spectrometer for lipid, peptide, and intact protein analysis in rat brain tissue. It transfers established on-tissue digestion and protein imaging protocols from a MALDI-7090 TOF-TOF system to the compact platform and evaluates its capability to detect and localize biomolecules up to 22 kDa.

Methodology


Sagittal sections of rat brain were mounted on ITO slides and subjected to a six-step solvent wash to remove salts and lipids. Samples were divided for on-tissue digestion or intact protein imaging. Porcine trypsin and CHCA matrix were applied for peptide generation, while sinapinic acid was used for intact proteins. Matrices were deposited using SunCollect and IMLayer AERO sprayers. Imaging was performed at 50 micrometer resolution in linear mode, and data were processed with IonView software.

Instrumentation Used


  • Shimadzu MALDI-8020 benchtop linear TOF mass spectrometer
  • Shimadzu MALDI-7090 TOF-TOF mass spectrometer
  • SunCollect sprayer (SunChrom)
  • IMLayer AERO spraying device (Shimadzu)
  • IonView data analysis software

Main Results and Discussion


Lipid imaging of rat brain yielded high-quality pseudo-color distributions correlating to anatomical structures. On-tissue digestion produced characteristic peptides from myelin basic protein localized to white matter and distinct signals in grey matter. Intact protein analysis detected neurogranin (m/z 7537), ubiquitin (m/z 8565), myelin basic protein (m/z 14124), and brain acid soluble protein I (m/z 22104), with spatial patterns matching tissue architecture. Despite the absence of MS/MS, peptide assignments based on accurate mass were consistent with in silico digests.

Benefits and Practical Applications


The compact and cost-effective MALDI-8020 system enables in situ peptide and protein imaging without the need for high-end instrumentation. Its robustness and user-friendly workflow make it suitable for teaching laboratories, small research facilities, and routine QA/QC environments.

Future Trends and Potential Applications


Advancements may include integration of tandem MS capabilities, enhanced mass resolution, automated sample preparation, and miniaturized platforms. Expanded applications could encompass clinical diagnostics, pharmacokinetics, biomarker discovery, and high-throughput tissue screening.

Conclusion


The study demonstrates that a low-cost benchtop MALDI-TOF instrument can effectively image peptides and proteins up to 22 kDa in tissue sections. The method offers a practical alternative for laboratories seeking accessible spatial proteomic analysis.

References


  1. Proceedings of the 68th ASMS Conference, Poster ThP225 (2020)
  2. Yang P et al (2011) Matrix sublimation/recrystallization for imaging proteins by mass spectrometry at high resolution. Analytical Chemistry 83:5728-5734
  3. Heijs B et al (2015) Brain region-specific dynamics of on-tissue protein digestion using MALDI mass spectrometry imaging. Journal of Proteome Research 14:5348-5354
  4. Franck J et al (2010) MALDI mass spectrometry imaging of proteins exceeding 30000 Da. Medical Science Monitor 16(9):BR293-299
  5. Schmitt N and Rawlins C (2019) Genetically encoded fluorescent proteins enable high-throughput assignment of cell cohorts directly from MALDI-MS images. Analytical Chemistry 91(6):3810-3817
  6. Groseclose MR et al (2007) Identification of proteins directly from tissue: in situ tryptic digestions coupled with imaging mass spectrometry. Journal of Mass Spectrometry 42:254-262

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