From: p53 amyloid aggregation in cancer: function, mechanism, and therapy
Inhibitor | Type | Targeting the p53 mutation site | Principle | Experiment |
---|---|---|---|---|
ReACp53[109] | A designed 17-residue peptide Inhibitor | Target R175 and R248 in HGSOC, have no effect on cells with folded wild-type p53 | p53 amyloid spine structure is used to design ReACp53 ((R9)RPILTRITLE). Targeting p53 segment 251–257 | In vitro and in vivo |
LI [110] | Bifunctional ligands | Y220C | Zn-free p53 exhibits accelerated protein aggregation, and LI modulate mutant p53 aggregation and restore zinc binding using a metallochaperone approach | In vitro and in vivo |
Tripyridylamide ADH-6[111] | Protein mimetic amyloid inhibitor | Target R175 and R248 in Pancreatic cancer, have no effect on cells with folded wild-type p53 | α-Helix mimetics are small molecules that imitate the topography of the most commonly occurring protein secondary structure, serving as effective antagonists of protein–protein interactions (PPIs) at the interaction interface | In vitro and in vivo |