Abstract: In the present application isolated peptides and aptamers thereof able to interact with structural and conformational p53 mutants within the region of the wild-type p53 DNA binding core domain comprised from amino acids 74 to amino acids 298 using the yeast two-hybrid method are disclosed. These PAs are able to efficiently recognize several different p53 point mutants but not wild-type p53. Therefore the peptides and aptamers identified can be useful as inhibitors of mutant p53-associated pro-oncogenic functions for anticancer therapy or as diagnostic tools for mut-p53 or wild-type p53 or as template for designing new peptido-mimetic drugs able to specifically target tumor cells.

Abstract: It is described the influence of the presence of mutations in the TP53 gene in association with high levels of the enzyme prolyl isomerase Pin1 and a molecular signature of 10 genes expression correlated with the expression of Pin1 and p53 for the prognosis of breast tumors. The association between overexpression of Pin1 and the presence of protein p53 mutants induces transcriptional programs which promote tumor aggressiveness and in a cohort of patients the overexpression of Pin1 has proved to influence the prognostic value of the presence of mutations in the gene TP53. The assessment of the expression of Pin1 in the presence of mutations of the gene TP53, together with the detection of the expression of the genes forming the molecular signature can therefore be used for the prognosis of breast cancer.

Abstract: Mutations in the p53 tumor suppressor gene are frequently found in human tumors and mutant p53 proteins actively collaborate with tumor progression. Interfering with mutant p53 function may represent a valid strategy to block tumor growth and development of aggressive phenotypes. As a consequence of the characteristic of peptide aptamers (PAs) to efficiently and selectively bind a target protein, they are able to interfere with its function and in its ability to interact with other partners. In the present application isolated peptides and aptamers thereof able to interact with structural and conformational p53 mutants within the region of the wild-type p53 DNA binding core domain comprised from amino acids 74 to amino acids 298 using the yeast two-hybrid method are disclosed. These PAs are able to efficiently recognize several different p53 point mutants but not wild-type p53.