Identification of interaction regions for protein-protein and antibody-antigen interactions

A profound understanding of protein structure and its interactions is crucial for revealing their biological functions. However, due to the complexity and diversity in the field of proteins, a single research technique often struggles to fully elucidate their mysteries. Therefore, biologists typically adopt a strategy of integrating multiple technical approaches to collectively explore the three-dimensional structure and dynamic interaction behaviors of proteins. Among these, cross-linking mass spectrometry (XL-MS) technology has demonstrated outstanding research value in this field due to its unique advantages. It can precisely provide spatial distance information between amino acid residues and has many advantages, such as requiring small sample amounts, low environmental requirements for proteins, no molecular weight limitations, ease of in situ cross-linking, simplicity of operation, and obtaining a large amount of information.

After more than twenty years of continuous development and technological innovation, XL-MS technology has made significant progress in experimental design, data analysis, and other aspects, and has now become an indispensable core tool in integrated structural biology. The XL-MS technology employed by Coalesce Bio utilizes different combinations of chemical cross-linking agents. These agents react with different amino acid residues such as carboxyl, amino, and sulfhydryl groups, enabling precise cross-linking of protein-protein and antibody-antigen interactions, thus accurately resolving interaction regions.

Technical Platform

Common chemical cross-linkers (as shown in the figure below) can covalently cross-link specific amino acid residues when added to protein systems. After enzymatic digestion, cross-linked peptides are generated, representing the interaction regions between proteins. Through mass spectrometry identification and precise analysis of the peptide sequences, information about the interaction regions can be obtained.

Amino-to-thiol cross-linker BS3

Amino-sulfhydryl crosslinker EMCS

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5. Cutting-Edge Equipment: Equipped with advanced mass spectrometers like the Thermo Fisher Orbitrap Exploris 480 and Bruker timsTOF, we facilitate groundbreaking research.

Our Service

Project	Identification of interaction regions for protein-protein and antibody-antigen interactions
Sample	Pure protein, antibody-antigen complex
Hardware Platform	Non-contact ultrasonic cell pulverizer，ChemiDoc MP Imaging System，Orbitrap Fusion Lumos Tribrid/Orbitrap Exploris 480/Q Exactive HF-X/timsTOF Pro 2 mass spectrometer
Project Duration	2-4 weeks
Deliverables	Project Report (including experimental procedures, data analysis charts, bioinformatics analysis results)
Price	Click to consult

Case Study

In this case, BSA serum protein was cross-linked using the amine-reactive cross-linker BS3 to construct a dimeric structure of BSA serum protein. Mass spectrometry analysis of the dimeric structure identified cross-linked peptide segments that matched existing literature data, thereby validating the accuracy and reliability of the experiment.