Home LiteratureArticle Details
PMID: 42348942 Published · ppublish English

A novel ERα-targeted hydrophobic tag degrader, overcomes tamoxifen resistance via unfolded protein response-induced apoptosis and homologous recombination repair inhibition in breast cancer.

Bioorganic chemistry ·Vol. 180 ·2026-09-15

Shen R, Xin L, Liu J, Li K, Deng X, Liu X, Wang C, Min J, Zhou HB, Huang J

Abstract

Breast cancer (BC), predominantly ERα-positive, often develops resistance to endocrine therapy. We designed 20a, a novel ERα degrader based on the OBHSA scaffold with a hydrophobic amantadine tag. This compound demonstrates potent efficacy against both tamoxifen-sensitive and -resistant BC models in vitro and in vivo, with minimal systemic toxicity. Structural analysis reveals that 20a induces conformational changes in ERα (helixes 11-12), facilitating Hsp70 recruitment and subsequent ubiquitin-proteasome degradation. Additionally, 20a activates the ATF4-CHOP axis of the unfolded protein response, inducing apoptosis, while impairing homologous recombination repair through RAD51 degradation and BRCA1/2 downregulation. The latter effect creates synthetic lethality with Olaparib. Our findings elucidate the multi-mechanistic antitumor profile of 20a, highlighting its potential as a next-generation therapeutic for endocrine-resistant ERα-positive BC.

Keywords
Breast cancer Endocrine resistance Estrogen receptor Hydrophobic tagging Unfolded protein response
Article Info
Journal
Bioorganic chemistry
Abbr.
Bioorg Chem
ISSN
1090-2120
Published
2026-09-15
Language
English
Country/Region
United States
NLM ID
1303703
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com