Relationships leading to the potent VHL inhibitor VH298

The article will be part of the journal Special Issue on “Inducing Protein Degradation as a New Therapeutic Strategy”, edited by Prof. Craig Crews and Prof. Shameng Wang.

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Crystal structure of VH298 bound to VHL
Crystal structure of VH298 bound to VHL
Table of content graphics
Table of content graphics
Figure 1. Initial optimization strategy
Figure 1. Initial optimization strategy
Figure 2. Biophysical characterization of inhibitor 10 binding to VBC.
Figure 2. Biophysical characterization of inhibitor 10 binding to VBC.
Figure 3. Co-crystal structures of first-series inhibitors
Figure 3. Co-crystal structures of first-series inhibitors
Figure 4. Cellular activity and toxicity of 10
Figure 4. Cellular activity and toxicity of 10
Figure 5. Second series optimization strategy.
Figure 5. Second series optimization strategy.
Figure 6. Inhibitor 15 is not cytotoxic.
Figure 6. Inhibitor 15 is not cytotoxic.
Figure 7. Co-crystal structures of second-series inhibitors
Figure 7. Co-crystal structures of second-series inhibitors
Figure 8. Correlations between cellular activity and physicochemical parameters in vitro
Figure 8. Correlations between cellular activity and physicochemical parameters in vitro
Figure 9. Activity in cells vs half-life dissociation from VBC protein complex.
Figure 9. Activity in cells vs half-life dissociation from VBC protein complex.
Scheme 1
Scheme 1
Scheme 2
Scheme 2
Scheme 3
Scheme 3


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