Quantitative Proteomics: SILAC for SM-Protein Interactions

This lecture delves into quantitative proteomics using SILAC to identify small-molecule (SM)-protein interactions. The experimental design involves light and heavy amino acid labeling, incubation with SM-loaded beads, and analysis of MS spectra. The limitations, controls, and interpretations of the results are discussed, along with the significance of specific binding patterns. Various tools and concepts in chemical biology are explored, including enzyme inhibitors, target ID methods, and proteome-level signaling analysis. A case study on competitive ABPP illustrates the application of covalent inhibitors and ABPP in studying enzyme activity and cancer proteomes.