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Methods for Inhibiting Chaperone Proteins

Posted Jun 14 2010 5:00pm 1 Comment

Description of Invention:
This invention is directed to depletion of the Heat Shock Protein (HSP)-90 with novobiocin. Hsp90 is an essential and abundant chaperone in eukaryotes. It is considered today an exciting molecular target for cancer therapy. NIH inventors demonstrated previously that the gyrase-B inhibitor, novobiocin, and its related coumarin derivatives interact with Hsp90, causing in vitro and in vivo depletion of key regulatory Hsp90-dependent proteins. Using deletion/mutation analysis, the inventors have identified the novobiocin binding domain on Hsp90 and demonstrated that it overlaps a functional ATP binding site, which was previously unknown. These results identify a second site on Hsp90 where the binding of small molecule inhibitors can significantly impact this chaperone’s function, and thus support the hypothesis that both N- and C-terminal domains of Hsp90 interact to modulate chaperone activity. The inventors have performed preliminary in vivo experiments, treating mice carrying tumor xenografts with novobiocin encapsulated in Alzet pumps (slow, constant release for one month). The treated mice exhibited significantly slower tumor growth. Results of these studies demonstrated a significantly slower growth of tumors.

Monica G Marcu (NCI)
Leonard M Neckers (NCI)
Theodor W Schulte (NCI)

Cancer - Therapeutics
In-vivo Data

For Additional Information Please Contact:
Admin. Licensing Spec-Cancer
NIH Office of Technology Transfer
6011 Executive Blvd. Suite 325,
Rockville, MD 20852
United States
Phone: 301-496-7057
Fax: 301-402-0220

Ref No: 447

Updated: 06/2010

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