Abstract 2776 Mechanistic insights into the dissociation kinetics of molecular chaperone Hsp90 inhibitors

Heat shock protein 90 (Hsp90) is a ubiquitous molecular chaperone that supports the folding and maturation of numerous proteins in the eukaryotic cytosol. Its clients include many oncogenic proteins-such as kinases, hormone receptors, and transcription factors-that are crucial for signal transduction and cellular regulation. The survival of cancer cells is therefore heavily reliant on Hsp90, making it a promising target for cancer therapy. Although over 60 clinical trials for Hsp90 inhibitors are currently in progress, only one, TAS-116, has received approval (for the treatment of gastrointestinal stromal tumors in Japan).