Inhibition of p53 protein aggregation as a cancer treatment strategy

The p53 protein plays a critical role in the prevention of genome mutations in the body, however, this protein is frequently mutated in cancer and almost all cancers exhibit malfunction along the p53 pathway. In addition to a loss of activity, mutant p53 protein is prone to unfolding and aggregation, eventually forming amyloid aggregates. There continues to be a considerable effort to develop strategies to restore normal p53 expression and activity and this review details recent advances in small-molecule stabilization of mutant p53 protein and the design of p53 aggregation inhibitors.

Automated summary

The p53 protein plays a crucial role in preventing genome mutations, but it is often mutated in cancer, leading to malfunction in the p53 pathway. Mutant p53 protein not only loses its activity, but also tends to unfold and aggregate, forming amyloid aggregates. This review discusses recent advancements in developing small-molecule stabilizers of mutant p53 protein and inhibitors of p53 aggregation.