Adimab scientists have developed a yeast-displayed synthetic library of llama-derived heavy chain–only antibodies (HCAbs) that provides a modular and adaptable framework for targeting a broad range of antigens without the need for light chains. Our platform accelerates discovery by generating high-quality HCAbs with strong binding, excellent stability, and suitability for therapeutic formats such as bispecifics and T cell engagers.
Highlights and features from the work:
- A synthetic HCAb library built using humanized frameworks and diverse complementarity-determining regions (CDRs) achieved broad antigen coverage while maintaining favorable biophysical characteristics.
- Yeast-surface presentation was used to enable rapid, high-throughput selection under multiple pressures, including affinity, expression, and specificity.
- Screening campaigns identified antigen-specific HCAbs across both soluble and membrane targets, demonstrating the platform’s flexibility and robustness.
- Top-performing antibodies were evaluated for expression yield, thermostability, aggregation resistance, and specificity, confirming that they met stringent developability standards.
- Outputs from the anti-CD28 HCAb screen were successfully reformatted into multispecific architectures that retained activity, stability, and favorable developability properties.
This synthetic, yeast-based HCAb platform provides a flexible backbone for next-generation molecule design, enabling quick access to high-performance heavy chain–only binders. Its versatility positions it as a foundational tool for constructing bispecifics, T cell engagers, and other advanced antibody-like modalities.
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