Discovery of novel Hsp90 C-terminal domain inhibitors that disrupt co-chaperone binding.

摘要: Heat shock protein 90 (Hsp90) is an essential molecular chaperone that performs vital stress-related and housekeeping functions in cells a current therapeutic target for diseases such as cancers. Particularly, the development of Hsp90 C-terminal domain (CTD) inhibitors highly desirable N-terminal nucleotide-binding may cause unwanted biological effects. Herein, we report on discovery two drug-like novel CTD by using virtual screening intrinsic fluorescence quenching binding assays, paving way future new therapies employ inhibitors.