ALiCE, produced in a 2-by-1 format, is designed to mainly target the surface of cancer cells in the body, as the tumor antigen-binding titers were increased to levels much higher than that of the CD3 antibody. Also, by lowering the binding affinity of the CD3 antibody, excessive T cell activation in the blood has been minimized.

As a typical Y-shaped IgG-type bispecific antibody, antibody modification based on structural engineering is minimized, making ALiCE a platform technology with the most natural bispecific antibody structure.


The upper portion of ALiCE, which maintains the structure of general antibodies, consists of bivalent Fab regions that recognize a target antigen on cancer cells. The crystallizable fragment (Fc) region of the antibody, however, is substituted with a monovalent variable fragment (Fv) region from a CD3-targeting antibody

ALiCE first binds to the target antigen on the surface of cancer cells through high affinity, bivalent binding. ALiCE then binds to CD3 present on CD8+ cytotoxic T cells near the cancer cell, resulting in the formation of an immune synapse and stimulating the T cell to become activated to kill the cancer cell even without the TCR-MHC binding signal.