Systematic format exploration enables therapeutic optimization 

Multispecific antibodies (msAbs) extend the therapeutic reach of antibody drugs by simultaneously engaging multiple targets. However, engineering them to be safe, stable, and developable requires exploring many format combinations—a process that conventional assembly methods make prohibitively slow. Our integrated platform provides an efficient, data-driven solution for generating diverse, developable msAbs at scale. 

Yeast-based discovery for fully human antibodies 

Our proprietary yeast display platform enables direct selection of fully human msAbs in native formats, eliminating the need for subsequent humanization. This approach generates antibodies with minimal non-human sequence while maintaining optimal binding kinetics and stability from the start, accelerating progression to therapeutic evaluation. 

Orthogonal pairing for clean assembly 

Engineered constant region interfaces enable reliable construction of msAbs with precise chain pairing. Our computationally designed CH1:Cκ and CH3 mutations ensure correct heterodimerization without chain mispairing or homodimer contamination, simplifying manufacturing and improving therapeutic quality from drug substance forward.

Correct assembly of multispecific antibodies

Generation of complex tetravalent msAbs. Orthogonal pairing sets, including κ and λ light chain–specific sets and CH3:CH3 heterodimerization, ensure correct assembly.

Chain Exchange technology for format diversity 

Redox-driven heavy chain exchange enables high-throughput generation of correctly paired msAbs without complex purification. ChEx reduces conventional transfection requirements from 144 individual attempts to just 24, enabling systematic exploration of geometry and valency combinations to find the architecture that optimizes function for your targets. 

Results at a glance 

  • Rapid format exploration: Systematic generation of diverse multispecific architectures exploring different valencies and geometries across CD28×TAA combinations. Format screening enabled identification of architectures with optimized target engagement. 
  • High purity without purification bottlenecks: All-Fab msAb designs achieve 90-95%+ purity post-Protein A purification. ChEx-generated heterodimers demonstrate 95-97% purity with confirmed dual-antigen binding by orthogonal analytical methods. 
  • Geometry-driven functional optimization: Identical binders in different msAb architectures show up to 24% differences in target cell binding, demonstrating that format geometry directly impacts biological activity and enabling rational selection of lead candidates. 

Accelerated development timeline  

From initial discovery through format optimization and analytical characterization, typical programs conclude within 6–9 months, yielding a panel of stable, high-purity, highly functional msAb leads ready for therapeutic assessment.