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Discovery of novel 2-azabicyclo[3.2.1]octane derivatives against non-small cell lung cancer from aconitine simplification.

Bioorganic chemistry 2026 Vol.168() p. 109360

Guo S, Li TT, Ge GH, Hu H, Xue WH, Wang YP, Zhang X, Liu HY, Liang JW, Zhang Y, Meng FH, Zhang TJ

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Aconitine, a diterpenoid alkaloid, exhibits promising bioactivities, but its clinical application is limited by severe toxicity.

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APA Guo S, Li TT, et al. (2026). Discovery of novel 2-azabicyclo[3.2.1]octane derivatives against non-small cell lung cancer from aconitine simplification.. Bioorganic chemistry, 168, 109360. https://doi.org/10.1016/j.bioorg.2025.109360
MLA Guo S, et al.. "Discovery of novel 2-azabicyclo[3.2.1]octane derivatives against non-small cell lung cancer from aconitine simplification.." Bioorganic chemistry, vol. 168, 2026, pp. 109360.
PMID 41386066

Abstract

Aconitine, a diterpenoid alkaloid, exhibits promising bioactivities, but its clinical application is limited by severe toxicity. Through a structural simplification and derivatization strategy, we designed and synthesized a novel series of 2-azabicyclo[3.2.1]octane derivatives. This effort culminated in the identification of compound 8q, which demonstrated potent and selective anti-tumor efficacy against ALK (anaplastic lymphoma kinase) -positive cancer cells (NCI-H2228 and Karpas-299), significantly outperforming ceritinib in enzymatic and cellular assays. Mechanism studies revealed that 8q effectively inhibits ALK phosphorylation and its downstream PI3K/AKT/mTOR and RAS/MEK/ERK signaling pathways, inducing G0/G1 phase cell cycle arrest and apoptosis. Moreover, 8q markedly suppressed cancer cell migration and invasion. In an NCI-H2228 xenograft model, 8q exhibited dose-dependent tumor growth inhibition, with the high-dose group (60 mg/kg) showing superior efficacy to ceritinib (30 mg/kg) and no significant systemic or organ toxicity. Molecular docking and dynamics simulations revealed that 8q stably binds within the ATP-binding pocket of ALK, forming key interactions with residues in the hinge (Glu1197) and solvent-front (Glu1269 and Asp1270) regions. The RMSD and RMSF analyses confirmed enhanced conformational stability of the 8q-ALK complex compared to the apo protein. Collectively, these findings highlight 8q as a promising lead compound for the development of novel ALK inhibitors with a favorable efficacy and safety profile.

MeSH Terms

Humans; Antineoplastic Agents; Cell Proliferation; Drug Screening Assays, Antitumor; Structure-Activity Relationship; Carcinoma, Non-Small-Cell Lung; Lung Neoplasms; Dose-Response Relationship, Drug; Molecular Structure; Animals; Mice; Drug Discovery; Apoptosis; Aconitine; Protein Kinase Inhibitors; Cell Line, Tumor; Molecular Docking Simulation; Azabicyclo Compounds; Mice, Nude; Anaplastic Lymphoma Kinase; Neoplasms, Experimental; Mice, Inbred BALB C

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