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

doi:10.1002/cbic.201100524

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 journal › Article › peer-review

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 language	English
Pages (from-to)	97-104
Number of pages	8
Journal	ChemBioChem
Volume	13
Issue number	1
DOIs	https://doi.org/10.1002/cbic.201100524
State	Published - Jan 2 2012
Externally published	Yes

Keywords

DNA
Heat shock proteins
Inhibition
Polyamides
Transcription factors

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10.1002/cbic.201100524

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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.",

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AU - Pandita, Raj K.

AU - Cai, Jianfeng

AU - Hunt, Clayton R.

AU - Taylor, John Stephen

PY - 2012/1/2

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N2 - 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.

AB - 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.

KW - DNA

KW - Heat shock proteins

KW - Inhibition

KW - Polyamides

KW - Transcription factors

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JO - ChemBioChem

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ER -

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

Abstract

Keywords

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