Publications

Gambogic Acid Inhibits Hsp90 and Deregulates TNF-alpha/NF-kappaB in HeLa Cells

Zhang, L., et al., 403(3-4), 282-287, Biochem Biophys Res Commun, 2010

Molecular docking, together with the Octet RED platform and spectroscopic methods, were used to study the interaction between a novel small molecule drug called Gambogic Acid (GB) and full-length Hsp90, N-Hsp90, M-Hsp90 and C-Hsp90. Biotinylated protein targets (e.g., Hsp90) were immobilized onto Super Streptavidin biosensors for interaction studies. From the binding energy and dissociation constants, the authors deduce that GB is an inhibitor of Hsp90 and that it binds to the N-terminal ATP-binding domain of Hsp90.

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