I present a de novo protein binder designed to neutralize the Nipah virus by targeting the G glycoprotein (PDB: 2VSM) at its critical receptor-binding interface. My strategy focuses on blocking the interaction with the Ephrin-B2 receptor by occupying the conserved hydrophobic pocket formed by residues Trp504, Phe458, and Leu305 with a high-affinity, computationally generated scaffold. To achieve this, I employed a state-of-the-art generative pipeline starting with RFdiffusion to generate 50-80 residue backbones constrained to these hotspots, followed by ProteinMPNN for sequence design with cysteine exclusion to ensure solubility.