Artesunate-binding FABP5 promotes apoptosis in lung cancer cells via the PPARγ-SCD pathway.

Artesunate holds excellent promise for lung cancer treatment, but its target is still unclear. We used molecular docking techniques to predict artesunate and Fatty acid binding protein 5 (FABP5) binding sites. Cellular thermal shift assay (CETSA) verified that artesunate treatment could promote the stability of the FABP5 protein. There was no significant change in the strength of the FABP5 protein after the mutation of binding sites by adding artesunate treatment. Mechanistically, artesunate promotes apoptosis in lung cancer cells by binding to FABP5, inhibiting the expression of the lipid metabolism gene SCD, and suppressing the expression of the SCD transcription factor regulated by the transcription factor PPARγ. In summary, our study shows that the protein targeted by artesunate is FABP5 and that artesunate promotes apoptosis through the FABP5-PPARγ-SCD pathway, which offers excellent potential for treating lung cancer.