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Author Notes:

Correspondence: Aiming Sun, Phone: 404-727-6689; Fax: 404-727-6689; Email: asun2@emory.edu

Acknowledgments: We gratefully acknowledge National Cancer Institute (NCI) for the generously supplying the samples listed in Fig 3.


Research Funding:

This work was financially supported by the US National Institutes of Health 1 U54 HG003918-02 and 1R03MH076499-01.


  • Heat Shock Protein 90 (Hsp90)
  • high-throughput screening (HTS)
  • aminoquinoline

Discovery of Aminoquinolines as a New Class of Potent Inhibitors of Heat Shock Protein 90 (Hsp90): Synthesis, Biology and Molecular Modeling

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Journal Title:

Bioorganic and Medicinal Chemistry


Volume 16, Number 14


, Pages 6903-6910

Type of Work:

Article | Post-print: After Peer Review


The molecular chaperone Hsp90 plays important roles in maintaining the 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 been 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.

Copyright information:

Published by Elsevier Ltd.

This is an Open Access work distributed under the terms of the Creative Commons Attribution-NonCommerical-NoDerivs 3.0 Unported License (http://creativecommons.org/licenses/by-nc-nd/3.0/).

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