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. Author manuscript; available in PMC: 2019 Apr 8.
Published in final edited form as: Biochim Biophys Acta Gen Subj. 2017 May 8;1861(8):1992–2006. doi: 10.1016/j.bbagen.2017.05.006

Fig. 7.

Fig. 7.

Inhibition of Hsp90 CTD chaperone activity is driven by BPA di-(2-hydroxyethyl)ether. A) Structure of NSC145366 and four symmetrical analogs (A1, A2, A3 and A8); all contain the same Bisphenol A (BPA) di-(2-hydroxyethyl) ether core but differ in their terminal moieties. B) Inhibitor activity of the analogs in the ADH chaperone assay. Cm A1 = coumermycin A1. All assays used identical conditions including 500 nM of Hsp90 CTD. *significant between untreated (Hsp90 C-terminus alone) and compound treated groups P ≤ 0.02 ‡significant between NSC145366 and analog groups P ≤ 0.003.