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

Rongsheng E. Wang, Raj K. Pandita, Jianfeng Cai, Clayton R. Hunt, John Stephen Taylor

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

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 β-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.

Original languageEnglish (US)
Pages (from-to)97-104
Number of pages8
JournalChemBioChem
Volume13
Issue number1
DOIs
StatePublished - Jan 2 2012

Keywords

  • DNA
  • Heat shock proteins
  • Inhibition
  • Polyamides
  • Transcription factors

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry

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