Journal
CHEMBIOCHEM
Volume 13, Issue 1, Pages 97-104Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201100524
Keywords
DNA; heat shock proteins; inhibition; polyamides; transcription factors
Funding
- NIH [PO1 CA 104457]
- Washington University [P41 RR000954]
- 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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