SN-38-A2

SN-38-A2 (48 h) exhibits potent antiproliferative activity in MIA PaCa-2, HCT116, and MCF-7 cancer cell lines, with IC₅₀ values of 10.4 nM, 5.9 nM, and 53.4 nM, respectively, and is ~10-fold more potent than SN-38 in HCT116 cells^[1].
SN-38-A2 (10-100 nM) induces concentration-dependent TOP1 degradation in MIA PaCa-2 cells, achieving ~61.5% TOP1 reduction at 10 nM and exhibiting superior degradation efficiency compared to SN-38-A1 and SN-38^[1].
SN-38-A2 mediates TOP1 degradation in MIA PaCa-2 cells predominantly through the ubiquitin-proteasome system, with HSP90 chaperone system involvement, and does not rely on lysosomal pathways^[1].
SN-38-A2 (50 nM; 24 h) causes significant, specific downregulation of TOP1 and remodeling of the cellular proteome, with enrichment of ubiquitin-proteasome pathway-related proteins, while leaving TOP2A and TOP2B levels unchanged^[1].
SN-38-A2 binds to the TOP1-DNA cleavage complex with a conserved intercalative mode, maintaining high-affinity interactions with the protein and DNA, while projecting its adamantane tag into the solvent-exposed vestibule to trigger degradation^[1].
SN-38-A2 forms stable, uniform, pH-responsive nanoparticles with PCD, achieving improved aqueous solubility and colloidal stability with triggered release under acidic conditions^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.