IMAGE: Under normal conditions, native p53 protein is folded but when chemicals and/or high pressure are applied the protein may unfold and loose its 3D structure. During the unfolding process, p53… view more
Credit: Guilherme A. de Oliveira
It has long been known that abnormal changes in the p53 protein are associated with many cancers. In fact, the gene that codes the p53 protein is the one most frequently mutated in human cancers. The protein, known as the guardian of the genome, has the main role of suppressing tumor formation and in so doing it blocks cancer development. But once mutated, the p53 protein not only stops working as expected, it also acquires new functions and characteristics that are catastrophic for the cell.
One of the characteristics observed in mutated p53 is the tendency to form amyloid aggregates, which are structures that no longer display the protein original 3D conformation, stick together, and are resistant to degradation. These amyloid aggregates build up in the tissue, are very harmful, and present a pathogen-like behavior where mutants highjack normal counterparts and convert them into the amyloid form. These aggregates have been found in many cancer patients and in other protein-misfolding diseases
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