Mak, OW, Sharma, N, Reynisson, J and Leung, IKH (2021) Discovery of novel Hsp90 C-terminal domain inhibitors that disrupt co-chaperone binding. Bioorganic and Medicinal Chemistry Letters, 38 (127857). ISSN 0960-894X

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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.

Item Type: Article
Additional Information: The final version of this accepted manuscript and all relevant information can be found online at;
Uncontrolled Keywords: Hsp90; Molecular chaperone; Virtual screening; Inhibitor; Cancer
Subjects: R Medicine > R Medicine (General)
R Medicine > R Medicine (General) > R735 Medical education. Medical schools. Research
Divisions: Faculty of Medicine and Health Sciences > School of Pharmacy and Bioengineering
Related URLs:
Depositing User: Symplectic
Date Deposited: 05 Mar 2021 09:02
Last Modified: 18 Feb 2023 01:30

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