Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...
Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

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...
Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
Matrix-Assisted Laser Desorption Ionization (MALDI)01:08

Matrix-Assisted Laser Desorption Ionization (MALDI)

Matrix-assisted laser desorption ionization (MALDI) is a powerful analytical technique used in mass spectrometry. It enables the identification and characterization of various biomolecules, including proteins, peptides, nucleic acids, and carbohydrates. MALDI is an ionization technique, widely employed in biological and medical research, as well as in fields like pharmacology and biochemistry.The analyte of interest, a biomolecule or a mixture of biomolecules, is mixed with a suitable matrix...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The Knockout of PEX11a Results in Mild Peroxisomal Dysfunction and Lowered Cardiac Recovery Following Langendorff-Mediated Ischemia-Reperfusion in Mice.

Cells·2026
Same author

Mass Spectrometry Imaging of Lipid and Metabolite Distributions in Cysts of <i>Besnoitia besnoiti</i>-Infected Bovine Skin.

Journal of the American Society for Mass Spectrometry·2025
Same author

Glycolipidomics of Liver Flukes and Host Tissues during Fascioliasis: Insights from Mass Spectrometry Imaging.

ACS infectious diseases·2024
Same author

Metabolipidomic changes induced by dermal nickel penetration determined in an ex vivo porcine ear skin model.

Rapid communications in mass spectrometry : RCM·2024
Same author

Hepatic Topology of Glycosphingolipids in <i>Schistosoma mansoni</i>-Infected Hamsters.

Analytical chemistry·2024
Same author

<i>Schistosoma mansoni</i> infection induces hepatic metallothionein and S100 protein expression alongside metabolic dysfunction in hamsters.

PNAS nexus·2024

Related Experiment Video

Updated: Jul 12, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Data-Independent Acquisition for Improved Compound Annotation in MALDI MS Imaging.

Carmen Paschke1, Kerstin Strupat1, Carolin M Morawietz2,3

  • 1Thermo Fisher Scientific (Bremen) GmbH, Bremen 28199, Germany.

Journal of the American Society for Mass Spectrometry
|July 10, 2026
PubMed
Summary

This study introduces a new Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry Imaging (MALDI MSI) workflow using data-independent acquisition (DIA) to improve biomolecule mapping in tissues. The novel method enhances lipid identification and spatial metabolomics accuracy.

More Related Videos

Dithranol as a Matrix for Matrix Assisted Laser Desorption/Ionization Imaging on a Fourier Transform Ion Cyclotron Resonance Mass Spectrometer
09:38

Dithranol as a Matrix for Matrix Assisted Laser Desorption/Ionization Imaging on a Fourier Transform Ion Cyclotron Resonance Mass Spectrometer

Published on: November 26, 2013

Molecular Imaging of Human Brain Organoids Using Mass Spectrometry
08:04

Molecular Imaging of Human Brain Organoids Using Mass Spectrometry

Published on: September 27, 2024

Related Experiment Videos

Last Updated: Jul 12, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Dithranol as a Matrix for Matrix Assisted Laser Desorption/Ionization Imaging on a Fourier Transform Ion Cyclotron Resonance Mass Spectrometer
09:38

Dithranol as a Matrix for Matrix Assisted Laser Desorption/Ionization Imaging on a Fourier Transform Ion Cyclotron Resonance Mass Spectrometer

Published on: November 26, 2013

Molecular Imaging of Human Brain Organoids Using Mass Spectrometry
08:04

Molecular Imaging of Human Brain Organoids Using Mass Spectrometry

Published on: September 27, 2024

Area of Science:

  • Analytical Chemistry
  • Biochemistry
  • Metabolomics

Background:

  • Matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI MSI) is crucial for spatial biomolecule mapping in tissues.
  • Conventional methods often yield ambiguous compound annotations, and data-dependent acquisition (DDA) has limitations in specificity and reproducibility.
  • There is a need for improved MALDI MSI workflows that provide both spatial and fragmentation data for enhanced annotation.

Purpose of the Study:

  • To develop and validate a novel MALDI MSI workflow integrating data-independent acquisition (DIA) for improved spatial metabolomics.
  • To enhance the specificity and confidence of compound annotations in MALDI MSI data.
  • To demonstrate the workflow's utility in mapping biomolecules within biological tissues.

Main Methods:

  • A new MALDI MSI workflow was developed, alternating acquisition of MS¹ and data-independent acquisition (DIA) MS² spectra.
  • Small, randomized m/z isolation windows were employed in DIA MS² acquisition to reduce spectral overlap.
  • Data processing involved an extended Compound Discoverer, integrating mzCloud and LipidSearch for annotation, combining precursor-mass, DIA MS², and spatial correlation.

Main Results:

  • The workflow successfully generated detailed lipid maps for the parasitic worm *Fasciola hepatica* tissue.
  • Annotation confidence was significantly improved by integrating precursor-mass, DIA MS², and spatial-correlation information.
  • The approach provided high spatial resolution MS¹ data and broad m/z coverage with enhanced fragment-ion specificity.

Conclusions:

  • Data-independent acquisition (DIA) offers a flexible strategy to incorporate fragmentation information into MALDI MSI.
  • This integrated workflow expands the capabilities of MALDI MSI for high-confidence spatial metabolomics.
  • The method demonstrates potential for detailed biomolecular mapping in various biological tissues.