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Structure-based design improved binding affinity and safety profile in Nur77-Bcl-2-mediated apoptosis.
Nur77, a member of the NR4A nuclear receptor family, plays a critical role in tumorigenesis and cancer progression. Ligands activating its nongenomic functions hold therapeutic promise in oncology. Our previous work identified NB1, a 4,4'-bipyridyl cinnamamide derivative, as a novel Nur77 B-site ligand that induces mitochondrial translocation of Nur77 and triggers Nur77/Bcl-2-mediated apoptosis. Through structure-based optimization, we developed NF1 by replacing the 4-hydroxypiperidine group with an N-methylpentane moiety. This modification enhanced the compound's Nur77-binding affinity and stability. NF1 maintains a similar binding mode to NB1, effectively induced apoptosis via the Nur77-Bcl-2 pathway, and demonstrates significant in vivo antitumor efficacy, acceptable pharmacokinetics, and a high safety profile (LD₅₀ > 500 mg/kg). Collectively, these results establish NF1 as a promising candidate for further development in cancer therapy.
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Zhao et al. (2025) studied this question.
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