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Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

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...
Mass Spectrometry: Carboxylic Acid, Ester, and Amide Fragmentation01:01

Mass Spectrometry: Carboxylic Acid, Ester, and Amide Fragmentation

The fragmentation patterns observed for compounds such as carboxylic acids, esters, and amides in the mass spectra include ⍺-cleavage and McLafferty rearrangement. Fragmentation by ⍺-cleavage preferentially occurs at the carbon-carbon bond at the ⍺-position next to the carboxylic group to generate a neutral radical and a cation. Long chain compounds with hydrogen at their γ-carbon undergo McLafferty rearrangement to give a radical cation and a neutral alkene.
For example, the fragmentation of...

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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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Mass Spectrometry-Based Structural Characterization and Reaction Kinetics Profiling of Stapled Peptides through

Zijian Gong1, Yuexiang Sun2,1, Yuqing Sun3

  • 1Shandong Laboratory of Yantai Drug Discovery, Bohai Rim Advanced Research Institute for Drug Discovery, Yantai, Shandong 264117, China.

Analytical Chemistry
|June 18, 2026
PubMed
Summary

A new mass spectrometry (MS) platform precisely analyzes stapled peptides, overcoming challenges in structural heterogeneity. This method aids in optimizing macrocyclic peptide therapeutics by clarifying connectivity and reaction pathways.

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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
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Published on: April 14, 2015

Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Medicinal Chemistry

Background:

  • Peptide stapling enhances macrocyclic peptide therapeutics but often yields complex mixtures.
  • Analyzing stapled peptide connectivity and macrocyclization selectivity is challenging.

Purpose of the Study:

  • To develop a mass spectrometry (MS)-based platform for detailed structural analysis of stapled peptides.
  • To enable mechanistic interrogation of stapled peptide formation pathways.
  • To facilitate characterization and optimization of macrocyclic peptide therapeutics.

Main Methods:

  • Utilized MS-grade proteases for controlled enzymatic linearization of stapled macrocycles.
  • Integrated ion mobility spectrometry for separation and quantification of regioisomeric products.
  • Employed covalent labeling to localize modification sites on stapled peptides.

Main Results:

  • Developed a platform for structural elucidation of stapled peptides and their formation pathways.
  • Achieved separation and quantitative monitoring of regioisomeric stapled products.
  • Enabled direct assessment of site-selective macrocyclization kinetics.
  • Demonstrated localization of modification sites within complex stapled peptide systems.

Conclusions:

  • The developed platform provides systematic analysis of stapling connectivity, topology, and reaction selectivity.
  • Offers a valuable tool for characterizing and optimizing macrocyclic peptide therapeutics.
  • Addresses limitations in analyzing structurally heterogeneous stapled peptide products.