Refining Potent STAT3 Inhibitor Structure Through Molecular Docking
Location
OC Auditorium
Start
4-2-2026 2:10 PM
Type of Presentation
Oral Presentation
Abstract
Signal Transducer and Activator of Transcription 3 (STAT3) is constitutively activated in cancers such as glioblastoma and triple negative breast cancer, making it a key therapeutic target. Current inhibitors often act on upstream pathways, which cancer cells can bypass, highlighting the need for inhibitors that directly bind STAT3 at core domains. This study investigates derivatives of the compound IX-11 using molecular docking with SwissDock and AutoDock Vina against STAT3 (PDB: 1BG1). Structural modifications included nitro group substitution, cyclohexanone core alteration, and halogen variation. Replacing nitro groups with nitrogen-rich heteroaromatic rings improved predicted binding via hydrogen bonding and π-stacking. Addition of an N-acetyl group enhanced stability, while removal of the central ring reduced affinity. Fluorine outperformed chlorine and bromine as a substituent. The top candidate combined oxadiazole substitution with an acetamide group. These results provide structure–activity insights supporting future synthesis and experimental validation of direct STAT3 inhibitors.
Refining Potent STAT3 Inhibitor Structure Through Molecular Docking
OC Auditorium
Signal Transducer and Activator of Transcription 3 (STAT3) is constitutively activated in cancers such as glioblastoma and triple negative breast cancer, making it a key therapeutic target. Current inhibitors often act on upstream pathways, which cancer cells can bypass, highlighting the need for inhibitors that directly bind STAT3 at core domains. This study investigates derivatives of the compound IX-11 using molecular docking with SwissDock and AutoDock Vina against STAT3 (PDB: 1BG1). Structural modifications included nitro group substitution, cyclohexanone core alteration, and halogen variation. Replacing nitro groups with nitrogen-rich heteroaromatic rings improved predicted binding via hydrogen bonding and π-stacking. Addition of an N-acetyl group enhanced stability, while removal of the central ring reduced affinity. Fluorine outperformed chlorine and bromine as a substituent. The top candidate combined oxadiazole substitution with an acetamide group. These results provide structure–activity insights supporting future synthesis and experimental validation of direct STAT3 inhibitors.