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<p>Heat shock proteins (HSPs) play a major role in cell survival in response to stress. Cancer cells in particular rely on these chaperone proteins to facilitate their proliferation and survival. Heat shock factor 1 (HSF1), a transcription factor, sits at the center of this pathway controlling downstream HSP regulation. HSF1, itself, is upregulated in response to heat or stress. As a result, cancer cells have elevated levels of HSF1 relative to healthy cells, and therefore the inhibition of HSF1 has potential to be a promising cancer treatment. HSF1 acts by binding to DNA thus triggering downstream regulation. This study describes the use of a fluorescence polarization assay that interrogates the DNA-binding domain of HSF1. This FP assay was used to demonstrate the suitability toward high throughput screening and the discovery of a new scaffold for HSF1 inhibition.</p><p></p>

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Discovery and development of inhibitors of heat shock factor 1 by a fluorescence polarization assay

  • 期刊论文

  • 发表日期：

    2025年12月12日

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  • Geoffrey H. Chan,
  • Matthew J. Moschitto

摘要

Heat shock proteins (HSPs) play a major role in cell survival in response to stress. Cancer cells in particular rely on these chaperone proteins to facilitate their proliferation and survival. Heat shock factor 1 (HSF1), a transcription factor, sits at the center of this pathway controlling downstream HSP regulation. HSF1, itself, is upregulated in response to heat or stress. As a result, cancer cells have elevated levels of HSF1 relative to healthy cells, and therefore the inhibition of HSF1 has potential to be a promising cancer treatment. HSF1 acts by binding to DNA thus triggering downstream regulation. This study describes the use of a fluorescence polarization assay that interrogates the DNA-binding domain of HSF1. This FP assay was used to demonstrate the suitability toward high throughput screening and the discovery of a new scaffold for HSF1 inhibition.