Journal
BIOORGANIC & MEDICINAL CHEMISTRY
Volume 20, Issue 11, Pages 3609-3614Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2012.03.067
Keywords
Hsp70; J-Domain co-chaperones; Luciferase refolding; Thermal shift analysis
Funding
- Alzheimer's Drug Discovery Foundation
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Inhibitors of both heat shock proteins Hsp90 and Hsp70 have been identified in assays measuring luciferase refolding containing rabbit reticulocyte lysate or purified chaperone components. Here, we report the discovery of a series of phenoxy-N-arylacetamides that disrupt Hsp70-mediated luciferase refolding by binding to DnaJ, the bacterial homolog of human Hsp40. Inhibitor characterization experiments demonstrated negative cooperativity with respect to DnaJ and luciferase concentration, but varying the concentration of ATP had no effect on potency. Thermal shift analysis suggested a direct interaction with DnaJ, but not with Hsp70. These compounds may be useful tools for studying DnaJ/Hsp40 in various cellular processes. (C) 2012 Elsevier Ltd. All rights reserved.
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