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Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Published on: March 9, 2010

BiPS, a photocleavable, isotopically coded, fluorescent cross-linker for structural proteomics.

Evgeniy V Petrotchenko¹, Kunhong Xiao, Jennifer Cable

¹Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599, USA.

Molecular & Cellular Proteomics : MCP

|October 8, 2008

Summary

A novel photocleavable, fluorescent, and isotopically coded cross-linker, BiPS, simplifies protein structure analysis. This method enables sensitive detection and identification of cross-linked peptides using mass spectrometry, advancing structural and cellular biology.

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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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Published on: November 28, 2017

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Last Updated: Jun 29, 2026

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Published on: March 9, 2010

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Area of Science:

Proteomics
Structural Biology
Biochemistry

Background:

Mass spectrometry and cross-linking are crucial for studying protein structure and interactions.
Identifying cross-linked peptides post-digestion remains a significant challenge in proteomics.

Purpose of the Study:

To introduce a novel cross-linker, bimane bisthiopropionic acid N-succinimidyl ester (BiPS), designed to overcome existing limitations.
To demonstrate the utility of BiPS in protein structure and interaction studies.

Main Methods:

Utilized BiPS, a photocleavable, fluorescent, homobifunctional, amine-reactive, and isotopically coded cross-linker.
Employed gel electrophoresis, HPLC, and mass spectrometry (MALDI-MS, tandem MS) for analysis.
Developed automated software for cross-link identification and classification.

Main Results:

BiPS's fluorescence enabled sensitive monitoring of cross-linking, protein isolation, and peptide separation.
Isotopic coding generated characteristic mass spectrometry ion signal doublets for easy detection.
Photocleavage facilitated differentiation of cross-link types and peptide sequencing.
Provided direct evidence for a phosphorylated G-protein-coupled receptor C terminus docking site on beta-arrestin.

Conclusions:

BiPS offers a versatile and powerful tool for cross-linking mass spectrometry.
The unique properties of BiPS significantly enhance the identification and characterization of cross-linked peptides.
This approach has broad potential applications in structural and cellular biology research.