Disruption of Focal Adhesion Kinase and p53 Interaction with Small Molecule Compound R2 Reactivated p53 and Blocked Tumor Growth

Golubovskaya V, et al., 13(1), 342, BMC Cancer, 2013

The authors identified a small molecule (R2) that bound to Focal Adhesion Kinase (FAK), disrupted the binding of FAK and p53, and decreased cancer cell viability and clonogenicity in a p53-dependent manner. The Octet RED384 system was used for binding studies. Human FAK-N-terminal domain protein was biotinylated and loaded onto Super Streptavidin biosensors for the characterization of R2-FAK binding. For detection of FAK-p53 dissociation by R2, p53 protein was biotinylated and bound to Streptavidin biosensors.

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