Surface Plasmon Resonance Imaging-MALDI-TOF Imaging Mass Spectrometry of Thin Tissue Sections

Identification and quantification of proteins in imaging of biological samples are a challenge in today’s science. Here, we demonstrate a novel surface plasmon resonance imaging-matrix assisted laser desorption ionization imaging mass spectrometry (SPRi-MALDI IMS) coupled technique competent for the...

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Bibliographic Details
Published in:Analytical chemistry (Washington) 2016-02, Vol.88 (4), p.2072-2079
Main Authors: Forest, Simon, Breault-Turcot, Julien, Chaurand, Pierre, Masson, Jean-Francois
Format: Article
Language:English
Subjects:
Animals
Correlation
Correlation analysis
Desorption
Diffusion
Diffusion rate
Imaging
Kidney - metabolism
Liver - metabolism
Mass spectrometry
Mice
Plasmons
Proteins
Proteins - chemistry
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Surface chemistry
Surface Plasmon Resonance
Tissues
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Summary:Identification and quantification of proteins in imaging of biological samples are a challenge in today’s science. Here, we demonstrate a novel surface plasmon resonance imaging-matrix assisted laser desorption ionization imaging mass spectrometry (SPRi-MALDI IMS) coupled technique competent for the acquisition of multiparametric information by creating a tissue section imprint on an SPRi sensor surface. Correlated images were acquired in SPRi and in MALDI IMS for abundant proteins from a single mouse kidney tissue. The spatial organization of the transferred proteins from the tissue to the SPRi surface was preserved and imaged by SPR and MALDI MS. Surface chemistry was selected to nonspecifically adsorb and retain high concentrations of proteins on the SPRi surface. The diffusion kinetics were controlled to ensure fast transfer of proteins from the tissue sections with minimal lateral diffusion to achieve high spatial fidelity transfer. Lastly, the SPRi instrument was modified to insert a tissue sample in the fluidics chamber to facilitate the real-time measurement of the transfer process. The MALDI IMS experimental conditions, such as matrix deposition and the interface between the SPRi prism and the MALDI IMS instrument, were also optimized. The results show quantitative and regioselective SPRi images correlating to MALDI IMS images of different proteins transferred from a single tissue section.
ISSN:0003-2700
1520-6882
DOI:10.1021/acs.analchem.5b03309