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The CD47-CD138 bispecific antibody is a preclinical therapeutic candidate designed for the treatment of multiple myeloma (MM). Developed by researchers at the Medical College of Wisconsin, this bispecific antibody (BsAb) utilizes a single-chain variable fragment (scFv) format, linking an anti-CD47 scFv with an anti-CD138 scFv via a human serum albumin (HSA) linker. The drug's mechanism of action involves dual-targeting: it binds to CD138 (Syndecan-1), which is highly and specifically expressed on multiple myeloma cells, and simultaneously blocks CD47, a "do not eat me" signal that inhibits phagocytosis by interacting with SIRP-alpha on macrophages. By preferentially binding to MM cells, the antibody aims to enhance tumor-specific phagocytosis while reducing the "sink effect" and off-target toxicities (such as anemia or T-cell depletion) typically associated with systemic CD47 blockade.
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