Cross-Linkers to Advance Protein-Protein Interaction Studies

Brief Description

A novel approach to studying protein-protein interactions using trioxane-based cross-linking mass spectrometry.

Full Description

This technology introduces a new suite of sulfoxide-containing, MS-cleavable cross-linking reagents that utilize trioxane as the cleavable site, enhancing the study of protein-protein interactions (PPIs) by allowing more flexible cross-linker design and improving the capture of PPIs in 3-D space. Through the use of DSTO, TSTO, and TDSTO cross-linkers, this method enables efficient, accurate, and robust identification of cross-linked peptides, providing crucial insights into the architecture of protein complexes without the need for cell engineering.

Suggested uses

• Structural biology research and protein complex architecture elucidation. 
• Drug discovery by targeting specific protein-protein interactions. 
• Biotechnological advancements in understanding cellular functionality and physiological states. 
• Development of novel therapeutic strategies based on the mechanistic functions of protein complexes.

Advantages

• Enables the capture of endogenous protein-protein interactions without cell engineering. 
• Provides distance constraints at specific residues, aiding in the refinement of protein structures. 
• Improves flexibility in cross-linker design with trioxane’s multiple extension sites. 
• Facilitates the identification of cross-linked peptides containing three individual peptides, offering additional structural information. 
• Ensures robust MS-cleavability for simplified identification in multistage tandem mass spectrometry analysis workflows.

Patent Status

Patent Pending