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Inhibition of Heat Shock Transcription Factor Binding by a Linear Polyamide Binding in an Unusual 1:1 Mode
Author(s) -
Wang Rongsheng E.,
Pandita Raj K.,
Cai Jianfeng,
Hunt Clayton R.,
Taylor JohnStephen
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201100524
Subject(s) - hsf1 , heat shock factor , heat shock protein , hsp70 , heat shock , transcription factor , in vitro , shock (circulatory) , microbiology and biotechnology , cytotoxic t cell , chemistry , biology , biophysics , biochemistry , gene , medicine
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.