Elena Johnson
A highly conserved molecular chaperon called Heat Shock Protein (HSP90) is required for the maturation of freshly generated polypeptides and offers a haven for the refolding or denatured protein turnover. The client proteins of HSP90 encompass the entire oncogenesis process, which is connected to all cancer hallmarks, in malignancies. The client proteins are directed for proteasomal destruction when their complexes with HSP90 are broken, according to mounting evidence. As a result, HSP90 and its co-chaperones have become promising targets for the creation of new cancer treatments. As a result, many natural compounds and their analogues that target HSP90 have been discovered. Through multiple routes, they have demonstrated a potent inhibitory effect on many cancer types. The inhibitors work by physically attaching to HSP90, its co-chaperones, or its client proteins. A number of HSP90 inhibitors are undergoing promising clinical trials, including shepherdin, geldanamycin, and its derivatives, gamitrinib and shepherdin. Here, we go through HSP90's subcellular location, its associated method of action in malignant phenotypes, and new developments in the creation of HSP90 inhibitors.