HER2-targeted antibody–drug conjugate composed of a humanized anti-HER2 IgG1 (disitamab) linked via a cleavable linker to the cytotoxic payload MMAE. After binding ERBB2 (HER2) on tumor cells and internalization, MMAE is released to inhibit tubulin polymerization, causing G2/M arrest and apoptosis; the Fc region may mediate ADCC and bystander killing.
Disitamab vedotin targets HER2 (ERBB2) on tumor cells; after binding and internalization, its cleavable linker releases the microtubule poison MMAE, which inhibits tubulin polymerization causing G2/M arrest and apoptosis. The IgG1 Fc may also mediate ADCC and enable bystander killing.
The ADC binds HER2, is internalized, and releases MMAE that inhibits tubulin polymerization, causing G2/M arrest and apoptosis; its IgG1 Fc can also recruit ADCC, with potential bystander killing from released MMAE.
Human IgG1 monoclonal antibody immune-checkpoint inhibitor targeting PD-L1; blocks PD-L1/PD-1 signaling to restore anti-tumor T-cell activity and can mediate Fc-dependent ADCC against PD-L1–positive tumor cells.
Avelumab is a human IgG1 monoclonal antibody that binds PD-L1, blocking its interaction with PD-1 to release inhibitory signaling on T cells and restore anti-tumor immunity; its intact Fc can also mediate antibody-dependent cellular cytotoxicity (ADCC) against PD-L1–expressing tumor cells.
Avelumab binds PD-L1 and, via its IgG1 Fc, engages FcγR-bearing effector cells (e.g., NK cells) to mediate ADCC against PD-L1–expressing cells; PD-1/PD-L1 blockade also restores T-cell killing.
Anti-HER2 monoclonal antibody that inhibits HER2/ERBB2 signaling and mediates antibody-dependent cellular cytotoxicity in HER2-positive tumor cells.
Humanized anti-HER2 (ERBB2) IgG1 monoclonal antibody that binds HER2 on tumor cells, inhibits HER2 signaling and proliferation, and induces antibody-dependent cellular cytotoxicity (ADCC) against HER2-overexpressing cells.
Trastuzumab binds HER2 on target cells and its Fc engages Fcγ receptors on effector cells (e.g., NK cells), triggering ADCC and lysis of HER2-positive cells.
An antibody–drug conjugate consisting of a humanized anti–Trop‑2 IgG1 linked via a cleavable linker to SN‑38 (the active metabolite of irinotecan, a topoisomerase I inhibitor). It binds Trop‑2 on tumor cells, is internalized, and releases SN‑38 to inhibit topoisomerase I, causing DNA damage and cell death, with potential bystander effect.
Humanized anti–Trop-2 IgG1 antibody linked via a cleavable linker to SN-38 (topoisomerase I inhibitor). After binding Trop-2 on tumor cells and internalization, SN-38 is released intracellularly to inhibit topoisomerase I, inducing DNA damage, cell-cycle arrest, and apoptosis; the cleavable linker can enable a bystander effect.
The ADC binds TROP-2, is internalized, and releases SN-38 (topoisomerase I inhibitor), causing DNA damage, cell-cycle arrest, and apoptosis; a cleavable linker can also enable a bystander effect.
Patient-derived T lymphocytes genetically engineered to express a chimeric antigen receptor that recognizes a tumor-associated antigen and activates T-cell effector functions via CD3ζ and a costimulatory domain (e.g., CD28 or 4-1BB), leading to cytotoxic killing, cytokine release, expansion, and persistence.
Autologous T lymphocytes are genetically engineered to express a chimeric antigen receptor that binds a tumor-associated antigen independent of MHC, initiating CD3ζ signaling with a costimulatory domain (e.g., CD28 or 4-1BB) to activate cytotoxic killing, cytokine release, proliferation, and persistence of the T cells to eliminate antigen-expressing tumor cells.
CAR T cells recognize the target antigen via the CAR and, upon CD3ζ/costimulatory signaling, directly kill antigen-positive cells through perforin–granzyme release and Fas–FasL–mediated apoptosis (with cytokine-mediated effects).