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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: Oct 18, 2025

A Hydrogen-Deuterium Exchange Mass Spectrometry HDX-MS Platform for Investigating Peptide Biosynthetic Enzymes

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Published on: May 4, 2020

A Novel UPLC-MS/MS Method Identifies Organ-Specific Dipeptide Profiles.

Elena Heidenreich¹, Tilman Pfeffer², Tamara Kracke²

¹Centre for Organismal Studies (COS), Metabolomics Core Technology Platform, Heidelberg University, 69120 Heidelberg, Germany.

International Journal of Molecular Sciences

|September 28, 2021

Summary

This summary is machine-generated.

This study reveals distinct organ-specific distribution patterns for 30 dipeptides in mice. Dipeptide levels varied significantly across tissues, offering new insights into dipeptide metabolism in health and disease.

Keywords:

UPLC biofluids dipeptides mass spectrometry metabolism tissue

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Last Updated: Oct 18, 2025

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Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

Area of Science:

Metabolomics
Biochemistry
Physiology

Background:

Amino acids are crucial for cell metabolism, with intracellular changes linked to disease pathogenesis.
The specific roles and organ distribution of dipeptides remain largely uncharacterized.

Purpose of the Study:

To establish a method for quantifying multiple dipeptides.
To investigate the organ-specific distribution of dipeptides in mice.
To correlate dipeptide profiles with amino acid profiles.

Main Methods:

Developed a sensitive UPLC-MS/MS method for quantifying 36 dipeptides.
Analyzed dipeptide patterns in various mouse tissues (adipose, brain, heart, kidney, liver, lung, muscle, etc.), serum, and urine.
Related dipeptide profiles to corresponding amino acid concentrations.

Main Results:

Detected 30 out of 36 dipeptides with significant organ-specific distribution.
Carnosine and anserine were most abundant, particularly in muscles.
Observed distinct dipeptide profiles in liver, spleen, thymus, and serum, with lower concentrations in serum.
Found higher concentrations of C-terminal proline dipeptides compared to N-terminal proline dipeptides.
Correlated tissue amino acid concentrations with specific dipeptide profiles.

Conclusions:

The developed multi-dipeptide quantification approach reveals organ-specific dipeptide distribution.
This methodology enhances understanding of dipeptide metabolism in both healthy and diseased states.