Resolving the Complexity of Spatial Lipidomics Using MALDI TIMS Imaging Mass Spectrometry

Journal article (2020)

Authors

Katerina V. Djambazova VanderBilt University
Dustin R. Klein VanderBilt University
L.G. Migas Team Raf Van de Plas - Mechanical, Maritime and Materials Engineering
Elizabeth K. Neumann VanderBilt University
Emilio S. Rivera VanderBilt University
Raf Van de Plas Team Raf Van de Plas - Mechanical, Maritime and Materials Engineering
Richard M. Caprioli VanderBilt University
Jeffrey M. Spraggins VanderBilt University
Research Group
Team Raf Van de Plas (Mechanical, Maritime and Materials Engineering) (TU Delft)
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Published Date

2020

Language

English

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Faculty

Mechanical, Maritime and Materials Engineering

Department

Delft Center for Systems and Control

Research Group

Team Raf Van de Plas

Abstract

Lipids are a structurally diverse class of molecules with important biological functions including cellular signaling and energy storage. Matrix-assisted laser desorption/ionization (MALDI) imaging mass spectrometry (IMS) allows for direct mapping of biomolecules in tissues. Fully characterizing the structural diversity of lipids remains a challenge due to the presence of isobaric and isomeric species, which greatly complicates data interpretation when only m/z information is available. Integrating ion mobility separations aids in deconvoluting these complex mixtures and addressing the challenges of lipid IMS. Here, we demonstrate that a MALDI quadrupole time-of-flight (Q-TOF) mass spectrometer with trapped ion mobility spectrometry (TIMS) enables a >250% increase in the peak capacity during IMS experiments. MALDI TIMS-MS separation of lipid isomer standards, including sn backbone isomers, acyl chain isomers, and double-bond position and stereoisomers, is demonstrated. As a proof of concept, in situ separation and imaging of lipid isomers with distinct spatial distributions were performed using tissue sections from a whole-body mouse pup.