This design set was generated using ProteinDJ (Papenfuss Lab) on the UNSW Katana HPC, targeting the Nipah virus G glycoprotein (NiV-G; residues A212–A600) at key receptor-binding interface hotspots A532, A557, and A559. The goal was to explore de novo binder scaffolds that complement this epitope while maintaining structural diversity and compactness. Designs were restricted to 10–199 amino acids and filtered for high predicted interface quality. Selected sequences represent the top ten models by predicted interface stability and novelty, with no significant homology to known NiV-G or ephrin-B2 sequences.