期刊
BIOORGANIC & MEDICINAL CHEMISTRY
卷 16, 期 14, 页码 6903-6910出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2008.05.047
关键词
heat shock protein 90 (Hsp90); high-throughput screening (HTS); aminoquinoline
资金
- NHGRI NIH HHS [1 U54 HG003918-02, U54 HG003918, U54 HG003918-02] Funding Source: Medline
- NIMH NIH HHS [1R03MH076499-01, R03 MH076499] Funding Source: Medline
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. Published by Elsevier Ltd.
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