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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: Jun 9, 2025

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

Optimizing SureQuant for Targeted Peptide Quantification: a Technical Comparison with PRM and SWATH-MS Methods.

Minia Antelo-Varela¹, Dirk Bumann¹, Alexander Schmidt¹

¹Biozentrum, University of Basel, Spitalstrasse 41, Basel CH-4056, Switzerland.

Analytical Chemistry

|October 28, 2024

Summary

This summary is machine-generated.

The SureQuant mass spectrometry method accurately quantifies scarce bacterial proteins in human samples. This technique enhances the detection of pathogens like Staphylococcus aureus, aiding in developing new infection control strategies.

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Last Updated: Jun 9, 2025

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

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Published on: August 17, 2015

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An HS-MRM Assay for the Quantification of Host-cell Proteins in Protein Biopharmaceuticals by Liquid Chromatography Ion Mobility QTOF Mass Spectrometry

An HS-MRM Assay for the Quantification of Host-cell Proteins in Protein Biopharmaceuticals by Liquid Chromatography Ion Mobility QTOF Mass Spectrometry

Published on: April 17, 2018

Area of Science:

Proteomics
Mass Spectrometry
Infectious Diseases

Background:

Bacterial infections pose a significant global health threat, necessitating improved understanding of pathogen physiology in human tissues.
Identifying and quantifying low-abundance bacterial proteins amidst abundant human proteins presents a major challenge for mass spectrometry-based proteomics.

Purpose of the Study:

To evaluate the SureQuant method for highly sensitive targeted mass spectrometry in analyzing bacterial proteins within human samples.
To optimize parameters for qualitative and quantitative protein analysis using SureQuant with Staphylococcus aureus as a model pathogen.

Main Methods:

Exploration of the SureQuant method for targeted mass spectrometry.
Evaluation of parameters such as target number and intensity thresholds for protein analysis.
Comparison of SureQuant performance against parallel reaction monitoring and data-independent acquisition methods.

Main Results:

SureQuant demonstrated equivalent quantitative performance to parallel reaction monitoring but enabled quantification of up to 400 targets.
The SureQuant method surpassed the sensitivity and quantification capabilities of global data-independent acquisition techniques.
Optimized MS parameters were provided for sensitive quantification of various peptide panel sizes.

Conclusions:

SureQuant offers a highly sensitive and precise approach for quantifying scarce bacterial proteins in complex biological matrices.
This method provides a foundation for analyzing clinical specimens and detecting low-abundant proteins in various research applications.
The findings support the development of novel strategies for controlling bacterial infections through enhanced proteomic analysis.