Abstract
PARP inhibitor development is on the rise as more PARP family members emerge as novel drug targets in diseases such as cancer, inflammation, and viral infection. Understanding a drug's mechanism of action and potential risks for toxicity requires proteome-wide characterization of both on- and off-target engagement. This review will highlight different methods to map out the protein interaction profile of a small molecule, using the clinically approved PARP inhibitors as a case study. The approaches discussed here will mainly focus on chemoproteomic workflows, using inhibitor bead-conjugates and photoaffinity labeling probes, but will also touch on the utility of biochemical assays. Collectively, these strategies have revealed new targets for PARP inhibitors beyond the expected PARP1/2, providing valuable insights for understanding mechanism of action, toxicity, and polypharmacology.
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