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Gel-assisted mass spectrometry imaging enables sub-micrometer spatial lipidomics

Author

Listed:
  • Yat Ho Chan

    (University of Illinois Chicago)

  • Koralege C. Pathmasiri

    (University of Illinois Chicago)

  • Dominick Pierre-Jacques

    (University of Illinois Chicago)

  • Maddison C. Hibbard

    (University of Illinois Chicago)

  • Nannan Tao

    (Bruker Daltonics)

  • Joshua L. Fischer

    (Bruker Daltonics)

  • Ethan Yang

    (Bruker Daltonics)

  • Stephanie M. Cologna

    (University of Illinois Chicago
    University of Illinois Chicago)

  • Ruixuan Gao

    (University of Illinois Chicago
    University of Illinois Chicago
    University of Illinois Chicago)

Abstract

A technique capable of label-free detection, mass spectrometry imaging (MSI) is a powerful tool for spatial investigation of native biomolecules in intact specimens. However, MSI has often been precluded from single-cell applications due to the spatial resolution limit set forth by the physical and instrumental constraints of the method. By taking advantage of the reversible interaction between the analytes and a superabsorbent hydrogel, we have developed a sample preparation and imaging workflow named Gel-Assisted Mass Spectrometry Imaging (GAMSI) to overcome the spatial resolution limits of modern mass spectrometers. With GAMSI, we show that the spatial resolution of MALDI-MSI can be enhanced ~3-6-fold to the sub-micrometer level without changing the existing mass spectrometry hardware or analysis pipeline. This approach will vastly enhance the accessibility of MSI-based spatial analysis at the cellular scale.

Suggested Citation

  • Yat Ho Chan & Koralege C. Pathmasiri & Dominick Pierre-Jacques & Maddison C. Hibbard & Nannan Tao & Joshua L. Fischer & Ethan Yang & Stephanie M. Cologna & Ruixuan Gao, 2024. "Gel-assisted mass spectrometry imaging enables sub-micrometer spatial lipidomics," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-49384-w
    DOI: 10.1038/s41467-024-49384-w
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    References listed on IDEAS

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    1. Yining Jiang & Batiste Thienpont & Vinay Sapuru & Richard K. Hite & Jeremy S. Dittman & James N. Sturgis & Simon Scheuring, 2022. "Membrane-mediated protein interactions drive membrane protein organization," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    2. Lu Li & Cuiji Sun & Yaoting Sun & Zhen Dong & Runxin Wu & Xiaoting Sun & Hanbin Zhang & Wenhao Jiang & Yan Zhou & Xufeng Cen & Shang Cai & Hongguang Xia & Yi Zhu & Tiannan Guo & Kiryl D. Piatkevich, 2022. "Spatially resolved proteomics via tissue expansion," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    3. Yunhao Bai & Bokai Zhu & John-Paul Oliveria & Bryan J. Cannon & Dorien Feyaerts & Marc Bosse & Kausalia Vijayaragavan & Noah F. Greenwald & Darci Phillips & Christian M. Schürch & Samuel M. Naik & Edw, 2023. "Expanded vacuum-stable gels for multiplexed high-resolution spatial histopathology," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
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