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How can the unique structure of the bispecific ABBV-383 impact its safety and efficacy?
Featured:
Shaji KumarDuring the 64th American Society of Hematology (ASH) Annual Meeting and Exposition, the Multiple Myeloma Hub was pleased to speak to Shaji Kumar, Mayo Clinic, Rochester, US. We asked, How can the unique structure of the bispecific ABBV-383 impact its safety and efficacy?
How can the unique structure of the bispecific ABBV-383 impact its safety and efficacy?
In this video interview, Kumar considers the structure of ABBV-383, a B-cell maturation antigen (BCMA)/CD3 targeted bispecific antibody. ABBV-383 is unique in that it contains two BCMA binding domains, as well as a low-affinity binding domain to CD3. Kumar considers how this unique structure allows for effective myeloma cell death as well as reducing off-target toxicity, then goes on to outline the results presented at ASH 2022 from the phase I trial entitled: A phase 1 first-in-human study of ABBV-383, a BCMA × CD3 bispecific T-cell-redirecting antibody, as monotherapy in patients with relapsed/refractory multiple myeloma. Kumar focuses on the optimal dosage as well as the safety and efficacy profiles as established in this trial.
