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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...

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Updated: Apr 8, 2026

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry

Published on: July 31, 2011

Quantifying epitope presentation using mass spectrometry.

Nathan P Croft¹, Anthony W Purcell¹, David C Tscharke²

¹Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3141, Australia.

Molecular Immunology

|June 30, 2015

Summary

This summary is machine-generated.

Quantifying cell surface MHC-bound epitopes (pMHC) is crucial for understanding T cell responses. New targeted mass spectrometry methods now allow direct, simultaneous measurement of pMHC levels, advancing antigen presentation research.

Keywords:

Antigen processing and presentation Epitope MHC Mass spectrometry

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Area of Science:

Immunology
Mass Spectrometry
Proteomics

Background:

Accurate quantification of MHC-bound epitopes (pMHC) is essential for T cell immunology.
Previous methods relied on limited monoclonal antibodies or peptide elution assays.
These traditional techniques faced challenges in scope and feasibility.

Purpose of the Study:

To develop novel methods for measuring pMHC molecules.
To enable simultaneous quantification of relative and absolute pMHC levels.
To overcome limitations of existing antigen presentation analysis techniques.

Main Methods:

Advancement of targeted mass spectrometry techniques.
Direct measurement of pMHC molecules on cell surfaces.
Simultaneous quantification of pMHC relative and absolute levels.

Main Results:

Successful implementation of targeted mass spectrometry for pMHC quantification.
Demonstrated ability to measure both relative and absolute pMHC levels directly.
Overcame limitations associated with antibody-dependent and peptide elution methods.

Conclusions:

Targeted mass spectrometry offers a powerful new approach for studying antigen presentation.
This technique provides direct and simultaneous measurement of pMHC molecules.
The findings have significant potential to impact the field of T cell immunology and antigen processing.