Proteome-Wide Monitoring of Drug Action in Living Cells Using a Novel Label-Free Solvent-Based Shift Assay.

ABSTRACT: Biophysical proteomics assays allow for proteome-wide, label-free monitoring of ligand-induced changes in protein structure and stability, offering insights into protein-ligand interactions and modulation of biophysical properties of cellular proteins. These assays exploit the principle that compound-induced alterations in structure or stability of proteins can be detected through changes in their susceptibility to denaturation. Here, we introduce solvent proteome profiling in cells (SPICE), which employs solvent-based denaturation of proteins under otherwise physiological conditions in intact cells. We characterized solvent-induced denaturation of proteins inside cells as distinct from that in cell extracts and validated SPICE by detecting known drug-target interactions for multiple compo

SUBMITTER: Steinbrunn D 

PROVIDER: S-EPMC12802111 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature