4.4 Article

Inhibition of Heat Shock Transcription Factor Binding by a Linear Polyamide Binding in an Unusual 1:1 Mode

Journal

CHEMBIOCHEM
Volume 13, Issue 1, Pages 97-104

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201100524

Keywords

DNA; heat shock proteins; inhibition; polyamides; transcription factors

Funding

  1. NIH [PO1 CA 104457]
  2. Washington University [P41 RR000954]
  3. Washington University NMR facility [RR1571501]

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Heat shock proteins (HSPs) are known to protect cells from heat, oxidative stress, and the cytotoxic effects of drugs, and thus can enhance cancer cell survival. As a result, HSPs are a newly emerging class of protein targets for chemotherapy. Among the various HSPs, the HSP70 family is the most highly conserved and prevalent. Herein we describe the development of a beta-alanine rich linear polyamide that binds the GGA heat shock elements (HSEs) 3 and 4 in the HSP70 promoter in an unusual 1:1 mode and inhibits heat shock transcription factor 1 (HSF1) binding in vitro.

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