Humanized IgG1 monoclonal antibody against the HER2 extracellular domain; inhibits receptor signaling/dimerization and mediates antibody-dependent cellular cytotoxicity (ADCC).
Humanized IgG1 monoclonal antibody that binds the HER2 extracellular domain, inhibits receptor dimerization/activation and downstream signaling, promotes receptor downregulation, and mediates antibody-dependent cellular cytotoxicity (ADCC) against HER2-overexpressing tumor cells.
NO
INDIRECT
Trastuzumab binds HER2 on tumor cells; its Fc engages CD16A on NK cells to trigger ADCC, killing HER2+ target cells. CD16A-expressing cells act as effectors and are not killed.
A HER2-targeting humanized monoclonal antibody conjugated via a cleavable linker to the topoisomerase I inhibitor deruxtecan (DXd); binds HER2, is internalized, and releases DXd to cause DNA damage with a bystander effect in HER2-expressing (including HER2-low) breast cancer.
Humanized anti-HER2 monoclonal antibody (trastuzumab) linked via a cleavable linker to the topoisomerase I inhibitor deruxtecan (DXd). After binding HER2 on tumor cells, the ADC is internalized and the linker is cleaved to release DXd, which inhibits topoisomerase I, causing DNA damage and cell death. The membrane-permeable payload produces a bystander effect that can kill adjacent HER2-expressing and HER2-low tumor cells.
YES
DIRECT
The ADC binds HER2, is internalized, and releases deruxtecan (DXd), a topoisomerase I inhibitor, causing DNA damage and apoptosis in the target cell; the membrane-permeable payload can also kill nearby cells (bystander effect).
A HER2-targeting humanized monoclonal antibody conjugated via a cleavable linker to the topoisomerase I inhibitor deruxtecan (DXd); binds HER2, is internalized, and releases DXd to cause DNA damage with a bystander effect in HER2-expressing (including HER2-low) breast cancer.
Humanized anti-HER2 monoclonal antibody (trastuzumab) linked via a cleavable linker to the topoisomerase I inhibitor deruxtecan (DXd). After binding HER2 on tumor cells, the ADC is internalized and the linker is cleaved to release DXd, which inhibits topoisomerase I, causing DNA damage and cell death. The membrane-permeable payload produces a bystander effect that can kill adjacent HER2-expressing and HER2-low tumor cells.
NO
INDIRECT
The ADC binds HER2 (not topoisomerase I), is internalized, and releases DXd, which inhibits topoisomerase I to cause DNA damage and death. Topoisomerase I is the payload’s enzymatic target, not the antigen that directs cell killing.
A TROP-2–targeting humanized monoclonal antibody linked via a hydrolyzable linker to SN-38, a topoisomerase I inhibitor; binds TROP-2, internalizes, and can release SN-38 extracellularly to induce DNA damage with a bystander effect in TROP-2–positive tumors.
Humanized monoclonal antibody targeting TROP-2 linked via a hydrolyzable linker to SN-38 (topoisomerase I inhibitor). Upon binding TROP-2 on tumor cells, the ADC is internalized and/or releases SN-38 extracellularly, causing DNA damage and cell death with a bystander effect in TROP-2–positive tumors.
YES
DIRECT
ADC binds TROP-2 on tumor cells and delivers SN-38 (topoisomerase I inhibitor) via internalization or local release, causing DNA damage and apoptosis; also enables bystander killing.
A TROP-2–targeting humanized monoclonal antibody linked via a hydrolyzable linker to SN-38, a topoisomerase I inhibitor; binds TROP-2, internalizes, and can release SN-38 extracellularly to induce DNA damage with a bystander effect in TROP-2–positive tumors.
Humanized monoclonal antibody targeting TROP-2 linked via a hydrolyzable linker to SN-38 (topoisomerase I inhibitor). Upon binding TROP-2 on tumor cells, the ADC is internalized and/or releases SN-38 extracellularly, causing DNA damage and cell death with a bystander effect in TROP-2–positive tumors.
NO
INDIRECT
SG targets TROP-2 on cells and delivers SN-38; the payload inhibits topoisomerase I to cause DNA damage and cell death (with a bystander effect). Killing is driven by TROP-2–mediated delivery, not by recognition of topoisomerase I expression itself.