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 | |
| State | Published - Jan 2 2012 |
Keywords
- Binding Sites/drug effects
- DNA-Binding Proteins/antagonists & inhibitors
- Heat Shock Transcription Factors
- Humans
- Molecular Structure
- Nylons/chemical synthesis
- Protein Isoforms/antagonists & inhibitors
- Structure-Activity Relationship
- Transcription Factors/antagonists & inhibitors