본문으로 건너뛰기
← 뒤로

Targeting the Interaction of NRF2 and β-TrCP with Molecular Glues.

2/5 보강
ACS chemical biology 2026 Vol.21(4) p. 635-642 Genomics, phytochemicals, and oxidat
Retraction 확인
출처
PubMed DOI OpenAlex 마지막 보강 2026-04-29
OpenAlex 토픽 · Genomics, phytochemicals, and oxidative stress Protein Degradation and Inhibitors 14-3-3 protein interactions

O Donovan DH, Winter-Holt J, Collie GW, Cuomo ME, McGarry DJ, Fox M

📝 환자 설명용 한 줄

Inhibiting the oncogenic driver NRF2 in non-small cell lung cancer (NSCLC) represents a promising yet challenging clinical opportunity.

이 논문을 인용하기

↓ .bib ↓ .ris
APA Daniel H. O Donovan, Jon Winter-Holt, et al. (2026). Targeting the Interaction of NRF2 and β-TrCP with Molecular Glues.. ACS chemical biology, 21(4), 635-642. https://doi.org/10.1021/acschembio.5c01006
MLA Daniel H. O Donovan, et al.. "Targeting the Interaction of NRF2 and β-TrCP with Molecular Glues.." ACS chemical biology, vol. 21, no. 4, 2026, pp. 635-642.
PMID 41910202 ↗

Abstract

Inhibiting the oncogenic driver NRF2 in non-small cell lung cancer (NSCLC) represents a promising yet challenging clinical opportunity. Small molecules that enhance the NRF2:β-TrCP interaction ("molecular glues") could hold therapeutic potential by promoting the ubiquitination and proteasomal degradation of NRF2. NRX-252114 is a molecular glue previously reported to promote the interaction between β-catenin and β-TrCP. We now find that NRX-252114 can also enhance the association between β-TrCP and NRF2 phosphodegron peptides. To leverage this novel interaction for the development of NRF2:β-TrCP molecular glues, we synthesized and evaluated a library of chemical analogues, guided by homology modeling and subsequently by X-ray crystallography. Surprisingly, structural elucidation of the NRF2:β-TrCP complex revealed occlusion of the presumed molecular glue binding pocket. This mechanistic insight explains the limited affinity enhancement for analogues of NRX-252114, and provides a structural rationale for the lack of NRF2 degradation in cells. Our findings broaden the scope of β-TrCP-targeted molecular glues, demonstrate that NRF2 is "glueable" at the peptide level, and provide mechanistic guidance for future efforts to target the pharmacologically elusive NRF2 pathway in cancer.

🏷️ 키워드 / MeSH 📖 같은 키워드 OA만

🏷️ 같은 키워드 · 무료전문 — 이 논문 MeSH/keyword 기반