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

Reynisson

Authors



Abstract

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

Acceptance Date Feb 5, 2021
Publication Date Feb 17, 2021
Publicly Available Date Mar 29, 2024
Journal Bioorganic and Medicinal Chemistry Letters
Print ISSN 0960-894X
Publisher Elsevier
DOI https://doi.org/10.1016/j.bmcl.2021.127857
Keywords Hsp90; Molecular chaperone; Virtual screening; Inhibitor; Cancer
Publisher URL https://www.sciencedirect.com/science/article/pii/S0960894X21000834?via%3Dihub