The tumor suppressor protein p53 plays a crucial role as the primary regulator of the cell cycle. It functions as a transcription factor, guiding the cell toward DNA repair, senescence, or apoptosis. However, when p53 mutates—a phenomenon observed in over 50% of cancer cases—it loses its “guardian of the genome” function and gains oncogenic properties that promote tumor progression. Our group has recently discovered that mutant p53 forms prion-propagating amyloid aggregates, where one misfolded protein serves as a template for others. This intriguing phenomenon, however, is not yet fully understood. In this study, we aim to characterize the formation of these aggregates, defining their functions, protein interactions, post-translational modifications, and prion mechanisms. We will also assess their contributions to tumor development. We aim to develop drug candidates that can modulate p53 aggregation, thereby establishing this phenomenon as a new pharmacological target for anti-cancer therapy.