Abstract
Described is the synthesis of three different fluorescein-tagged derivatives of a macrocycle, and their binding affinity to heat shock protein 90 (Hsp90). Using fluorescence polarization anisotropy, we report the binding affinity of these fluorescein-labeled compounds to Hsp90 in its open state and ATP-dependent closed state. We show that the compounds demonstrate a conformation-dependent preference for binding to the closed state.
Published by Elsevier Ltd.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / metabolism
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Binding Sites
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Depsipeptides / chemistry*
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Depsipeptides / metabolism
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Depsipeptides / pharmacology
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Fluorescein / chemistry
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HSP90 Heat-Shock Proteins / chemistry*
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HSP90 Heat-Shock Proteins / metabolism
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Molecular Structure
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Protein Binding / drug effects
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Protein Conformation
Substances
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Depsipeptides
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HSP90 Heat-Shock Proteins
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sansalvamide A
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Adenosine Triphosphate
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Fluorescein