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Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

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Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
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Multimodal Study of Murine Cardiovascular Remodeling: Four-Dimensional Ultrasound and Mass Spectrometry Imaging
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MS-DIAL 5 multimodal mass spectrometry data mining unveils lipidome complexities.

Hiroaki Takeda1,2, Yuki Matsuzawa1, Manami Takeuchi1

  • 1Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei-shi, Tokyo, 184-8588, Japan.

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MS-DIAL 5 enhances lipidomics by enabling detailed structural analysis and molecular localization using electron-activated dissociation (EAD) tandem mass spectrometry (MS) and MS imaging (MSI). This tool accurately identifies lipid structures and their positions, advancing lipid biology research.

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Area of Science:

  • Lipidomics
  • Metabolomics
  • Mass Spectrometry (MS)

Background:

  • Existing informatics tools for lipidomics and metabolomics have limitations in handling multimodal mass spectrometry data.
  • There is a need for software that supports structural annotations guided by the Lipidomics Standards Initiative.

Purpose of the Study:

  • To introduce MS-DIAL 5, a software for in-depth lipidome structural elucidation using electron-activated dissociation (EAD)-based tandem MS.
  • To enable determination of molecular localization through MS imaging (MSI) data.
  • To utilize a species/tissue-specific lipidome database with predicted collision-cross section values.

Main Methods:

  • Utilized optimized EAD settings (14 eV kinetic energy) for lipid structure delineation.
  • Applied MS-DIAL 5 to analyze authentic lipid standards and MS imaging data.
  • Investigated eye-specific phosphatidylcholines and supplemented HeLa cells for enzyme identification.

Main Results:

  • MS-DIAL 5 correctly delineated lipid structures for 96.4% of authentic standards.
  • Accurate assignment of sn-, OH-, and C=C positions was achieved for 78.0% of standards above 1 μM.
  • Identified glycerol 3-phosphate acyltransferase as a candidate enzyme for n-3 VLC-PUFA incorporation at the sn1 position.

Conclusions:

  • MS-DIAL 5, with optimized MS data acquisition, significantly improves lipid structure and localization understanding.
  • The workflow facilitates insights into lipid biology, particularly concerning very-long-chain polyunsaturated fatty acids (VLC-PUFAs).
  • Confirms the role of glycerol 3-phosphate acyltransferase in specific phospholipid modifications.