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Discovery of aminoquinolines as a new class of potent inhibitors of heat shock protein 90 (Hsp90): Synthesis, biology, and molecular modeling.

ABSTRACT: The molecular chaperone Hsp90 plays important roles in maintaining malignant phenotypes. Recent studies suggest that Hsp90 exerts high-affinity interactions with multiple oncoproteins, which are essential for the growth of tumor cells. As a result, research has focused on finding Hsp90 probes as potential and selective anticancer agents. In a high-throughput screening exercise, we identified quinoline 7 as a moderate inhibitor of Hsp90. Further hit identification, SAR studies, and biological investigation revealed several synthetic analogs in this series with micromolar activities in both fluorescent polarization (FP) assay and a cell-based Western blot (WB) assay. These compounds represent a new class of Hsp90 inhibitors with simple chemical structures.

SUBMITTER: Ganesh T 

PROVIDER: S-EPMC2553564 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature

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Discovery of aminoquinolines as a new class of potent inhibitors of heat shock protein 90 (Hsp90): Synthesis, biology, and molecular modeling.

Ganesh Thota T   Min Jaeki J   Thepchatri Pahk P   Du Yuhong Y   Li Lian L   Lewis Iestyn I   Wilson Larry L   Fu Haian H   Chiosis Gabriela G   Dingledine Raymond R   Liotta Dennis D   Snyder James P JP   Sun Aiming A  

Bioorganic & medicinal chemistry 20080527 14

The molecular chaperone Hsp90 plays important roles in maintaining malignant phenotypes. Recent studies suggest that Hsp90 exerts high-affinity interactions with multiple oncoproteins, which are essential for the growth of tumor cells. As a result, research has focused on finding Hsp90 probes as potential and selective anticancer agents. In a high-throughput screening exercise, we identified quinoline 7 as a moderate inhibitor of Hsp90. Further hit identification, SAR studies, and biological inv  ...[more]

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