Cross-Linking Proteomics Analysis

Cross-linking proteomics analysis uses cross-linking methods for proteomics research, mainly used to address issues in protein interaction studies. Cross-linking relies on cross-linkers forming chemical bonds between specific amino acid residues of two or more proteins, tightly binding interacting proteins together. This can maintain protein interactions and capture weak and transient protein interactions.

Cross-linking methods can be divided into in vivo and in vitro cross-linking, homobifunctional and heterobifunctional, as well as photo-reactive cross-linking, based on the reaction environment and the type of cross-linker. In vivo cross-linking occurs within cells, helping maintain protein activity and avoiding false positives to some extent. In vitro cross-linking occurs in cell lysates or protein samples, outside the control of the cellular environment. In vitro cross-linking offers more choices of cross-linker types and is more suitable for discovering more stable protein-protein interactions. Homobifunctional cross-linkers have two identical reactive groups and can recognize the same functional groups on proteins. Heterobifunctional cross-linkers have different reactive groups and can recognize different protein functional groups. Photo-reactive cross-linkers have both chemical cross-linking groups and photo-reactive cross-linking groups. The photo-reactive groups respond only to UV light, achieving cross-linking of interacting proteins through a two-step reaction: first cross-linking the thermally unstable active groups and then UV cross-linking the second protein group.

Biotech company Biotech Park uses Thermo Fisher's Q Exactive HF mass spectrometry platform combined with Nano-LC to offerCross-linking method for protein interaction analysis
Technical service packages allow high-sensitivity detection of in vivo transient protein interactions and in vitro low-affinity proteins. Custom cross-linking methods can be designed according to different project needs. Free consultation is welcomed!

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