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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: Dec 22, 2025

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

Solid-Phase Peptide Capture and Release for Bulk and Single-Molecule Proteomics.

Cecil J Howard¹, Brendan M Floyd², Angela M Bardo²

¹Department of Chemistry, University of Texas at Austin, 100 E. 24th Street, Austin, Texas 78712, United States.

ACS Chemical Biology

|May 5, 2020

Summary

This summary is machine-generated.

Researchers developed a novel solid-phase method for peptide purification and modification. This technique simplifies sample preparation for advanced proteomics, including single-molecule protein sequencing.

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Last Updated: Dec 22, 2025

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry

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Published on: January 13, 2023

Area of Science:

Proteomics
Biochemistry
Analytical Chemistry

Background:

Proteomics research faces challenges with sample purity and complex chemical derivatization steps.
Existing methods often require highly purified proteins, limiting broader application.
Advancements in single-molecule techniques necessitate improved peptide preparation strategies.

Purpose of the Study:

To develop a versatile solid-phase capture-release strategy for peptide processing.
To streamline proteolysis, purification, and chemical modification of peptides in a single pot.
To enable traceless reversal of peptide capture for sensitive downstream applications like single-molecule sequencing.

Main Methods:

A novel solid-phase resin was employed for simultaneous proteolysis, capture, and derivatization of peptides from HEK293T cell lysate.
Over 40,000 unique peptides were analyzed to assess capture biases.
The capture strategy was demonstrated to be reversible and suitable for fluorescent labeling and C-terminal derivatization.

Main Results:

The solid-phase method efficiently processed peptides from a complex cellular proteome.
Peptide capture biases were surveyed across a large number of unique peptides.
Traceless release of captured peptides was achieved, preserving integrity for sensitive analyses.
Successful fluorescent labeling and C-terminal derivatization were performed for fluorosequencing.

Conclusions:

The developed solid-phase capture-release strategy simplifies peptide preparation for proteomics.
This method is adaptable for both bulk and single-molecule proteomics applications.
The technique offers a robust solution for purifying and modifying peptides with minimal loss and contamination.