OnCo
ideasIdea

Degrade the damaged p53 protein rather than trying to repair it

Some faulty p53 proteins do not just stop protecting the cell; they actively help the cancer. Removing them entirely may be easier than fixing them.

Gain-of-function mutant p53 accumulates to high levels because it escapes MDM2-mediated turnover, and it drives invasion and chemoresistance in mouse models. A selective degrader exploiting the mutant's dependence on HSP90 or its distinct conformation could deplete it. Precedent: HSP90 inhibitors destabilise mutant p53 and prolong survival in mutant-p53 mouse models, but are too toxic; a targeted degrader would separate the effect from global chaperone inhibition.

Hypothesis
Selective depletion of gain-of-function mutant p53 reduces metastasis and restores chemotherapy sensitivity in mutant-p53 models without affecting wild-type p53 in normal tissue.
Rationale
Mutant p53 accumulation is a distinguishing feature of tumour cells, which gives a natural therapeutic index; degradation is the modality of choice for proteins whose function is structural rather than enzymatic.
What would test it
Degrader discovery against R175H and R273H with conformation-selective binders; validate in genetically engineered mutant-p53 mouse models measuring metastasis and chemosensitivity.
Maturity
speculative
Who has to act
research
Cost to try
Medium ($1M to $50M)
Years to first evidence
8
Bottlenecks it attacks
  • The undruggable drivers · The proteins that drive most cancers, such as MYC, mutant p53 and most RAS variants, still have no good drug.

Connected

4top