Revisiting silibinin as a novobiocin-like Hsp90 C-terminal inhibitor: Computational modeling and experimental validation

Highlights

  • Silibinin is computationally predicted to overlap the novobiocin-binding mode to the C-terminal domain (CTD) of Hsp90.
  • Silibinin diminishes the efficiency of Hsp90 CTD binding to its co-chaperone PPID/cyclophilin D in the low millimolar range.
  • Silibinin is a novobiocin-like Hsp90 inhibitor binding the CTD to alter Hsp90-co-chaperone-client interactions.
  • Silibinin structure avoids unwanted hepatotoxicity, thereby providing a path to develop new Hsp90 inhibitors.

https://www.sciencedirect.com/science/article/pii/S027869151930434X

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