Research Progress of Protein-Protein Interaction Based on Liquid Chromatography Mass Spectrometry

Protein-protein interactions are involved in the regulation of many biological processes in cells, and the mapping of protein-protein interaction networks is crucial for understanding complex biological processes. Liquid chromatography-mass spectrometry (LC-MS) can identify and quantify thousands of proteins simultaneously in complex organisms with its high sensitivity and accuracy. Therefore, after the enrichment, labeling or co-fractionation of target proteins, combined with LC-MS technology to identify proteins accurately and sensitively, such techniques have been widely used in the analysis of protein-protein interaction networks in the complex samples. There are LC-MS-based methods for studying protein-protein interactions, including dimity purification mass spectrometry (AP-MS), proximity-dependent biotinylation coupled to mass spectrometry (PDB-MS), chemical cross-linking with mass spectrometry (XL-MS) and co-fractionation mass spectrometry (CF-MS). This review discusses the mechanism, advantages and applications of these methods for the identification towards the protein-protein interactions in cells.