Oncogenic proteins in tumour cells rely on molecular chaperones such as Hsp90 for their proper folding and maturation1. Hsp90 is therefore a potential inhibition target for the development of new anticancer agents. The chaperoning activity of Hsp90 is regulated by ATP hydrolysis. ATP binds at the N-terminal domain of Hsp90. Herein, we report our work using virtual high-throughput screening and biophysical techniques in the identification and validation of new chemical scaffolds that binds the N-domain of Hsp902. Our work may provide insights into the development of new Hsp90 N-domain inhibitors.
References:
1. Mielczarek-Lewandowska A, Hartman ML, Czyz M. Inhibitors of HSP90 in melanoma. Apoptosis. 2020;25(1-2):12-28. doi:10.1007/s10495-019-01577-1
2. Huang R, Ayine-Tora DM, Muhammad Rosdi MN, Li Y, Reynisson J, Leung IKH. Virtual screening and biophysical studies lead to HSP90 inhibitors. Bioorganic Med Chem Lett. 2017;27(2):277- 281. doi:10.1016/j.bmcl.2016.11.059