Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 18, Issue 22, Pages 4157-4163Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d0ob00928h
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There are relatively few methods available for discovering inhibitors of the protein-protein interactions (PPIs) that hold together homo-oligomers. We envisioned that Differential Scanning Fluorimetry (DSF) might be a versatile way to discover this type of inhibitor because oligomers are often more thermally stable than monomers. Using the homo-heptameric chaperonin, Hsp60, as a model, we screened similar to 5000 diverse compounds in 384-well plates by DSF, revealing molecules that partially inhibited oligomerization. Because DSF does not require protein labeling or structural information, we propose that it could be a versatile way to uncover PPI inhibitors.
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