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.
Copyright © 2018 Elsevier Ltd. All rights reserved.
Publication types
-
Research Support, N.I.H., Extramural
MeSH terms
-
Biphenyl Compounds / chemical synthesis
-
Biphenyl Compounds / chemistry
-
Biphenyl Compounds / pharmacology
-
Cell Line, Tumor
-
Cell Proliferation / drug effects
-
Cyclohexanols / chemical synthesis
-
Cyclohexanols / chemistry
-
Cyclohexanols / pharmacology
-
HSP90 Heat-Shock Proteins / antagonists & inhibitors
-
HSP90 Heat-Shock Proteins / metabolism*
-
Humans
-
MCF-7 Cells
-
Novobiocin / chemical synthesis
-
Novobiocin / chemistry
-
Novobiocin / pharmacology
-
Piperidines / chemical synthesis
-
Piperidines / chemistry
-
Piperidines / pharmacology
-
Protein Domains
-
Structure-Activity Relationship
Substances
-
Biphenyl Compounds
-
Cyclohexanols
-
HSP90 Heat-Shock Proteins
-
Piperidines
-
Novobiocin
-
phenylcyclohexane