https://orcid.org/0000-0002-2295-8434
Figures & data
Table 1. Biparatopic antibodies in the clinic. Molecules are listed in chronological order by start of first clinical trial.
Figure 1. bpAb architectures evaluated in clinical trials.
Striped domains represent common light chain VLs or IgG4 Fcs. REGN5093-M114 contains an average of 3.2 non-specifically conjugated drugs per antibody. #MBS301 does not contain hexamerization enhancing mutations; *Drug to antibody ratios and conjugation sites differ from the shown example.
Figure 2. MoAs of bpAbs.
(a) Schematic representation of avid target binding by a bpAb in cis or trans. BpAbs can unlock new biological activities such as (b) dual-pathway inhibition, (c) locking of ectodomains in an enzymatically inactive state, or (d) biparatopic receptor targeting to form higher-order complexes and elicit agonism. (e) Alternatively, receptor and Fc domain clustering by bpAb binding in trans can result in fast internalization and lysosomal trafficking or strong effector function, in particular complement-dependent cytotoxicity.
