Figure 1
Figure 1. Schematic diagrams of DNL modules and structures. (A) The design for CH1-DDD2-Fab module. (B) The design for CH3-AD2-IgG modules. (C) The structure of CH1-DDD2-Fab as a dimer. (D) The structure of CH3-AD2-IgG as a monomer. (E) The structure of a bispecific hexavalent construct generated by DNL from reacting CH1-DDD2-Fab with CH3-AD2-IgG. (F) The interaction of the DDD2 and AD2 peptides. The variable domains for the heavy and light chains (VH + VL) are shown in green or orange. The constant domains of the heavy and light chains (CH + CL), the hinge (Hg), the 14-amino-acid residue (L14), and 9-amino-acid residue peptide linkers (L9) are shown in gray. The DDD2 and AD2 peptides are shown in blue and pink, respectively.

Schematic diagrams of DNL modules and structures. (A) The design for CH1-DDD2-Fab module. (B) The design for CH3-AD2-IgG modules. (C) The structure of CH1-DDD2-Fab as a dimer. (D) The structure of CH3-AD2-IgG as a monomer. (E) The structure of a bispecific hexavalent construct generated by DNL from reacting CH1-DDD2-Fab with CH3-AD2-IgG. (F) The interaction of the DDD2 and AD2 peptides. The variable domains for the heavy and light chains (VH + VL) are shown in green or orange. The constant domains of the heavy and light chains (CH + CL), the hinge (Hg), the 14-amino-acid residue (L14), and 9-amino-acid residue peptide linkers (L9) are shown in gray. The DDD2 and AD2 peptides are shown in blue and pink, respectively.

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