2. Academic Validation
  3. Exploiting polarity and chirality to probe the Hsp90 C-terminus

Exploiting polarity and chirality to probe the Hsp90 C-terminus

  • Bioorg Med Chem. 2018 Jul 23;26(12):3096-3110. doi: 10.1016/j.bmc.2018.04.028.
Leah K Forsberg 1,  Rachel E Davis 1,  Virangika K Wimalasena 1,  Brian S J Blagg 2
Affiliations

Affiliations

  • 1 Department of Chemistry and Biochemistry, University of Notre Dame, 305 McCourtney Hall, Notre Dame, IN 46556 USA.
  • 2 Department of Chemistry and Biochemistry, University of Notre Dame, 305 McCourtney Hall, Notre Dame, IN 46556 USA. Electronic address: [email protected].
PMID: 29720349 DOI: 10.1016/j.bmc.2018.04.028
Abstract

Inhibition of the HSP90 C-terminus is an attractive therapeutic approach for the treatment of Cancer. Novobiocin, the first HSP90 C-terminal inhibitor identified, contains a synthetically complex noviose sugar that has limited the generation of structure-activity relationships for this region of the molecule. The work described herein utilizes various ring systems as noviose surrogates to explore the size and nature of the surrounding binding pocket.

Figures