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Related Experiment Video

Updated: Jun 18, 2026

Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry
10:59

Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry

Published on: May 21, 2018

N-terminal enrichment: developing a protocol to detect specific proteolytic fragments.

Athena A Schepmoes1, Qibin Zhang, Brianne O Petritis

  • 1Pacific Northwest National Laboratory, Richland, Washington 99352, USA. athena.schepmoes@pnl.gov

Journal of Biomolecular Techniques : JBT
|December 2, 2009
PubMed
Summary

This study introduces a new proteomics method to identify specific protein fragments by blocking N-termini and enriching N-terminal peptides. This approach enhances the analysis of proteolytic events in biological systems and disease research.

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Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
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Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

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Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
11:54

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

Area of Science:

  • Biochemistry
  • Proteomics
  • Molecular Biology

Background:

  • Proteolytic processing is crucial for physiological functions and disease regulation.
  • Current mass spectrometry (MS)-based proteomics (
  • bottom-up
  • ) struggles to identify specific proteolytic fragments due to analyzing all peptides.
  • A need exists for methods to specifically identify proteolytic fragments.

Purpose of the Study:

  • To develop a robust protocol for the effective identification of specific proteolytic fragments.
  • To improve the characterization of proteolytic processing events.
  • To enhance the understanding of cancer biology and disease biomarkers.

Main Methods:

  • Utilized an acetylation reaction to block protein N-termini and lysine residues.
  • Employed amine-reactive silica-bond succinic anhydride beads for N-terminal peptide enrichment.
  • Compared acetic anhydride and propionic anhydride for lysine blocking efficiency and distinguishing modifications.

Main Results:

  • Both acetic and propionic anhydride demonstrated ~95% efficiency in blocking lysine residues.
  • Propionic anhydride enabled differentiation between in vivo acetylated and chemically tagged peptides.
  • Identified >300 unique N-termini peptides and known cleavage sites in mouse plasma.

Conclusions:

  • The developed protocol effectively enriches N-terminal peptides, reducing sample complexity and increasing analytical sensitivity.
  • This method holds significant potential for discovering novel proteolytic pathways.
  • The findings will advance the understanding of cancer biology and aid in biomarker discovery for various diseases.