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Mesa — JURA Bio, Inc.

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Peptide-HLA (pHLA) complexes display fragments of proteins from inside the cell on the cell surface — making previously "undruggable" intracellular targets accessible to antibody-based therapies. TCR-mimicking antibodies that bind these complexes are among the most challenging molecules to develop. To map the druggability landscape of this target class, we designed scaled, simultaneous experiments to answer a straightforward question: which pHLA targets are readily targetable by antibodies that have been previously observed in healthy humans? JURA de novo designed antibodies Antibodies observed in healthy humans Each of the 82 million designs was tested against all 100 pHLA targets simultaneously. Thanks to LIFT, we observed binding across all conditions in a single experiment—generating ground truth about what physically exists in antibody sequence space, not what a model predicts. Select a target to view detailed binding data, humanness scores, and developability metrics Traditional

⸻ CASE STUDY Massively scaled, massively multiplexed Direct wetlab observations of de novo designed human antibody scFvs with the HLA-A2-presented intracellular target space. Peptide-HLA (pHLA) complexes display fragments of proteins from inside the cell on the cell surface — making previously “undruggable” intracellular targets accessible to antibody-based therapies. TCR-mimicking antibodies that bind these complexes are among the most challenging molecules to develop. To map the druggability landscape of this target class, we designed scaled, simultaneous experiments to answer a…

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