Work

Identification of a New Scaffold for Hsp90 C-Terminal Inhibition

Year: 2013

Type: article

Abstract: Inhibition of Hsp90 C-terminal function is an advantageous therapeutic paradigm for the treatment of cancer. Currently, the majority of Hsp90 C-terminal inhibitors are derived from novobiocin, a natural product traditionally used as an antibiotic. Assisted by molecular docking studies, a scaffold containing a biphenyl moiety in lieu of the coumarin ring system found in novobiocin was identified for development of new Hsp90 C-terminal inhibitors. Initial structure-activity studies led to derivatives that manifest good antiproliferative activity against two breast cancer cell lines through Hsp90 inhibition. This platform serves as a scaffold upon which new Hsp90 C-terminal inhibitors can be readily assembled for further investigation.

Source: ACS Medicinal Chemistry Letters

DOI: 10.1021/ml400404s

Authors: Huiping Zhao, Elisabetta Moroni, Giorgio Colombo, Brian S. J. Blagg

Institutions: University of Kansas, Institute of Chemistry of Molecular Recognition

Language: English

Topic: Heat shock proteins research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funder: National Cancer Institute