Resolving the Complexity of Spatial Lipidomics Using MALDI TIMS Imaging Mass Spectrometry
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...
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| Vydáno v: | Analytical chemistry (Washington) Ročník 92; číslo 19; s. 13290 |
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| Hlavní autoři: | , , , , , , , |
| Médium: | Journal Article |
| Jazyk: | angličtina |
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United States
06.10.2020
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| ISSN: | 1520-6882, 1520-6882 |
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| 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
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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
backbone isomers, acyl chain isomers, and double-bond position and stereoisomers, is demonstrated. As a proof of concept,
separation and imaging of lipid isomers with distinct spatial distributions were performed using tissue sections from a whole-body mouse pup. |
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| AbstractList | 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.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. 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 / 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 backbone isomers, acyl chain isomers, and double-bond position and stereoisomers, is demonstrated. As a proof of concept, separation and imaging of lipid isomers with distinct spatial distributions were performed using tissue sections from a whole-body mouse pup. |
| Author | Rivera, Emilio S Klein, Dustin R Migas, Lukasz G Djambazova, Katerina V Van de Plas, Raf Caprioli, Richard M Neumann, Elizabeth K Spraggins, Jeffrey M |
| Author_xml | – sequence: 1 givenname: Katerina V surname: Djambazova fullname: Djambazova, Katerina V organization: Mass Spectrometry Research Center, Vanderbilt University, 465 21st Avenue S #9160, Nashville, Tennessee 37235, United States – sequence: 2 givenname: Dustin R surname: Klein fullname: Klein, Dustin R organization: Department of Biochemistry, Vanderbilt University, 607 Light Hall, Nashville, Tennessee 37205, United States – sequence: 3 givenname: Lukasz G orcidid: 0000-0002-1884-6405 surname: Migas fullname: Migas, Lukasz G organization: Delft Center for Systems and Control, Delft University of Technology, 2628 CD Delft, The Netherlands – sequence: 4 givenname: Elizabeth K orcidid: 0000-0002-6078-3321 surname: Neumann fullname: Neumann, Elizabeth K organization: Department of Biochemistry, Vanderbilt University, 607 Light Hall, Nashville, Tennessee 37205, United States – sequence: 5 givenname: Emilio S surname: Rivera fullname: Rivera, Emilio S organization: Department of Biochemistry, Vanderbilt University, 607 Light Hall, Nashville, Tennessee 37205, United States – sequence: 6 givenname: Raf orcidid: 0000-0002-2232-7130 surname: Van de Plas fullname: Van de Plas, Raf organization: Delft Center for Systems and Control, Delft University of Technology, 2628 CD Delft, The Netherlands – sequence: 7 givenname: Richard M surname: Caprioli fullname: Caprioli, Richard M organization: Department of Medicine, Vanderbilt University, 465 21st Avenue S #9160, Nashville, Tennessee 37235, United States – sequence: 8 givenname: Jeffrey M orcidid: 0000-0001-9198-5498 surname: Spraggins fullname: Spraggins, Jeffrey M organization: Department of Biochemistry, Vanderbilt University, 607 Light Hall, Nashville, Tennessee 37205, United States |
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| SubjectTerms | Animals Ion Mobility Spectrometry Lipidomics Lipids - analysis Mice Mice, Inbred C57BL Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
| Title | Resolving the Complexity of Spatial Lipidomics Using MALDI TIMS Imaging Mass Spectrometry |
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