Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

MALDI-TOF Mass Spectrometry

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 Spectrometry

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 Spectrometry

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)

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...

Mass Spectrometry: Complex Analysis

Mass Spectrometry: Complex Analysis

Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...

Mass Spectrometry: Overview

Mass Spectrometry: Overview

Mass spectrometry is an analytical technique used to determine the molecular mass and molecular formula of a compound. The basic principle of mass spectrometry is to generate ions from the analyte molecule and measure these ion abundances against their molecular mass. One common type of ionization, known as electron ionization or EI, bombards the analyte molecules in the gas phase with high-energy electron beams. The electron beams displace an electron from the molecule and leave behind a...

You might also read

Related Articles

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

Sort by

Same author

Medication for subcutaneous administration: Microbiological and physicochemical stability of drug formulations prepared in advance and stored in syringes.

Palliative care and social practice·2026

Same author

Antiparasitic triterpenic ester and ursolic acid lipid nanocapsule design, cytotoxicity, and permeability evaluation for oral delivery.

Frontiers in drug delivery·2026

Same author

Engineered protein nanoclusters reduce liver fibrosis and hepatocellular carcinoma in mice models.

Bioactive materials·2026

Same author

In honor of Prof. Véronique Préat.

Drug delivery and translational research·2026

Same author

Complex anionic and zwitterionic N-glycans in Drosophila melanogaster.

Biochimica et biophysica acta. General subjects·2026

Same author

Microglia encapsulation in nanozyme-loaded hydrogels: response to oxidative stress and inflammation.

Nanomedicine (London, England)·2026

Search research articles

Related Experiment Video

Updated: May 10, 2026

Low Molecular Weight Protein Enrichment on Mesoporous Silica Thin Films for Biomarker Discovery

Low Molecular Weight Protein Enrichment on Mesoporous Silica Thin Films for Biomarker Discovery

Published on: April 17, 2012

Analysis of microarrays by MALDI-TOF MS.

Ana Beloqui¹, Javier Calvo, Sonia Serna

¹CICbiomaGUNE, Biofunctional Nanomaterials Unit, Paseo Miramon 182, 20009 San Sebastian, Spain.

Angewandte Chemie (International Ed. in English)

|June 13, 2013

Summary

Researchers developed a novel method to print ligand libraries on indium-tin oxide (ITO) surfaces for biochemical analysis. This technique enables efficient enzyme specificity assignment and glycoform profiling.

Keywords:

lectins mass spectrometry microarrays proteomics transferases

More Related Videos

Using the Open-Source MALDI TOF-MS IDBac Pipeline for Analysis of Microbial Protein and Specialized Metabolite Data

Using the Open-Source MALDI TOF-MS IDBac Pipeline for Analysis of Microbial Protein and Specialized Metabolite Data

Published on: May 15, 2019

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

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

Related Experiment Videos

Last Updated: May 10, 2026

Low Molecular Weight Protein Enrichment on Mesoporous Silica Thin Films for Biomarker Discovery

Low Molecular Weight Protein Enrichment on Mesoporous Silica Thin Films for Biomarker Discovery

Published on: April 17, 2012

Using the Open-Source MALDI TOF-MS IDBac Pipeline for Analysis of Microbial Protein and Specialized Metabolite Data

Using the Open-Source MALDI TOF-MS IDBac Pipeline for Analysis of Microbial Protein and Specialized Metabolite Data

Published on: May 15, 2019

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

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

Area of Science:

Biochemistry
Analytical Chemistry
Materials Science

Background:

Ligand libraries are crucial for identifying molecular interactions.
Current methods for library analysis can be complex and time-consuming.
Surface immobilization techniques are key for high-throughput screening.

Purpose of the Study:

To develop a novel method for creating and analyzing ligand libraries.
To demonstrate the utility of this method for biochemical applications.
To enable efficient assignment of enzyme specificity and profiling of glycoforms.

Main Methods:

Printing activated lipid-based ligand libraries onto a hydrophobic layer conjugated to an indium-tin oxide (ITO) surface.
Utilizing fluorescence spectroscopy for array analysis.
Employing mass spectrometry for detailed molecular identification.

Main Results:

Successfully created functional ligand arrays on ITO surfaces.
Demonstrated the capability of the arrays for analyzing enzyme specificity.
Showcased the profiling of glycoforms and identification of lectins using the developed platform.

Conclusions:

The developed printing technique provides a robust platform for ligand library creation and analysis.
This method offers a versatile tool for various biochemical applications, including specificity assignment and glycoform profiling.
The combination of surface immobilization and advanced spectroscopy facilitates high-throughput molecular discovery.