Rania Awad

In the human body, there are countless networks solely comprised of interactions between proteins. These complexes are known as protein-protein interaction (PPI) networks. PPI networks are regulated by a network of other proteins known as chaperones and co-chaperones, which facilitate proper protein folding and functioning. The collection of the chaperones, co-chaperones, and other factors helpful to protein function is known as the chaperome, a structure vital to maintaining proper bodily function. However, when disease applies stress to the body, the chaperome becomes rewired into a scaffold for misfolded, harmful proteins. The Chiosis Lab at the Memorial Sloan Kettering Cancer Center has named these disease-supporting complexes epichaperomes. The lab believes that collapsing or restructuring these protein complexes can return PPI networks to their normal state and, thus, return the body to a pre-disease condition. One of the main ways the lab has targeted these harmful protein complexes is by using the chemical compounds they have developed. These probes precisely attach only to the epichaperome proteins so that healthy proteins are not affected in the process. So far, this methodology has proven to be successful in treating many cancers—such as pancreatic cancer and breast cancer. The main probe used by the lab for cancer treatment is known as PU-H71, and it precisely targets the protein Hsp90 within the epichaperome. The lab has also begun to test whether epichaperome targeting can also be applied to neurodegenerative diseases—such as Alzheimer’s disease. Ultimately, the goal of the Chiosis Lab is to use the new, innovative techniques they have used to study different diseases and, eventually, translate their findings from bench to bedside.