Progress in mass spectrometry approaches to profiling protein-protein interactions in the studies of the innate immune system
- PMID: 39380887
- PMCID: PMC11460538
- DOI: 10.1007/s42485-024-00156-6
Progress in mass spectrometry approaches to profiling protein-protein interactions in the studies of the innate immune system
Abstract
Understanding protein-protein interactions (PPIs) is pivotal for deciphering the intricacies of biological processes. Dysregulation of PPIs underlies a spectrum of diseases, including cancer, neurodegenerative disorders, and autoimmune conditions, highlighting the imperative of investigating these interactions for therapeutic advancements. This review delves into the realm of mass spectrometry-based techniques for elucidating PPIs and their profound implications in biological research. Mass spectrometry in the PPI research field not only facilitates the evaluation of protein-protein interaction modulators but also discovers unclear molecular mechanisms and sheds light on both on- and off-target effects, thus aiding in drug development. Our discussion navigates through six pivotal techniques: affinity purification mass spectrometry (AP-MS), proximity labeling mass spectrometry (PL-MS), cross-linking mass spectrometry (XL-MS), size exclusion chromatography coupled with mass spectrometry (SEC-MS), limited proteolysis-coupled mass spectrometry (LiP-MS), and thermal proteome profiling (TPP).
Keywords: Affinity purification mass spectrometry (AP-MS); Cross-linking mass spectrometry (XL-MS); Limited proteolysis-coupled mass spectrometry (LiP-MS); Protein–protein interactions; Proximity labeling mass spectrometry (PL-MS); Size exclusion chromatography coupled with mass spectrometry (SEC-MS); Thermal proteome profiling (TPP).
Conflict of interest statement
Declarations Conflict of interest The authors declare no competing interests.
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