Abstract
Heat shock protein 90 (Hsp90) is a molecular chaperone necessary for maintaining oncogenic transformation. There is substantial interest in developing novel agents that bind to the N-terminal of the chaperone. Here we report the synthesis and characterization of two fluorescent Hsp90 inhibitors and probe their use in an Hsp90 fluorescent polarization assay.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Binding, Competitive
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Fluorescent Dyes / chemical synthesis*
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Fluorescent Dyes / pharmacology
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HSP90 Heat-Shock Proteins / chemistry*
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HSP90 Heat-Shock Proteins / drug effects
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Kinetics
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Molecular Structure
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Structure-Activity Relationship
Substances
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Fluorescent Dyes
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HSP90 Heat-Shock Proteins