Tumor protein p63 (TP63) is a member of the TP53 protein between normal and tumor cells. Here, we modeled TP63–TP53CM family that are important for development and in tumor supprescomplex using computational approaches. We then used our modsion. Unlike TP53, TP63 is rarely mutated in cancer, but instead els to design peptides to disrupt the TP63–TP53CM interaction and different TP63 isoforms regulate its activity. TA isoforms (TAp63) restore antitumorigenic TAp63 function. In addition, we studied act as tumor suppressors, whereas DN isoforms are strong drivers of DN isoform oligomerization and designed peptides to inhibit its squamous or squamous-like cancers. Many of these tumors become oligomerization and reduce their tumorigenic activity. We show addicted to DN isoforms and removal of DN isoforms result in that some of our peptides promoted cell death in a TP63 highly cancer cell death. Furthermore, some TP53 conformational mutants expressed cancer cell line, but not in a TP63 lowly expressed cancer (TP53CM) gain the ability to interact with TAp63 isoforms and cell line. Furthermore, we performed kinetic–binding assays to inhibit their antitumorigenic function, while indirectly promoting validate binding of our peptides to their targets. Our computational tumorigenic function of DN isoforms, but the exact mechanism of and experimental analyses present a detailed model for the TP63–TP53CM interaction is unclear. The changes in the balance of TP63–TP53CM interaction and provide a framework for potential TP63 isoform activity are crucial to understanding the transition therapeutic peptides for the elimination of TP53CM cancer cells.
ASJC Scopus subject areas
- Cancer Research