NiV-G was analyzed to identify the optimal binding site for disturbance of Ephrin receptor interaction. Boltzgen was utilized in the design process generating around 7000 designs from which three was selected. The final designs target the disordered, loop-rich interface crucial for viral entry. Entries 1 and 2 are based on the same scaffold, with different interacting loop compositions, while Entry 3 has an alternative backbone to explore a different architectural core design. The selection was based on design evaluations of structural plausability and interface quality using Dunbrack Lab’s ipSAE following AlphaFold 3 predictions.
id: rapid-mole-ivy

Nipah Virus Glycoprotein G
0.76
81.27
--
9.9 kDa
92
id: strong-lynx-opal

Nipah Virus Glycoprotein G
0.77
79.63
--
10.0 kDa
92
id: vast-heron-rose

Nipah Virus Glycoprotein G
0.73
81.26
--
9.2 kDa
88