In this submission, BoltzGen was used to design nanobodies that would bind to the NiV-G protein. Nanobodies offer an optimal balance of high antibody-like affinity and superior developability features (small size, high stability, and cost-effective recombinant production). This approach (BoltzGen) utilizes nanobody structures as starting templates, designing the CDR region to improve binding, thereby introducing a structurally distinct, robust inhibitory motif. The underlying hypothesis is that by employing this advanced generative design method, the resulting scaffolded nanobodies will yield superior inhibitory potency and a more viable drug profile than other protein candidates, specifically by achieving higher affinity due to the enlarged, conformationally constrained binding surfaces created by the scaffolds and the rigid structure of the nanobodies, and overcoming the limitations of shorter proteins/peptides flexibility and short in vivo half-life, leading to candidates with greater stability, solubility, and manufacturing scalability.
id: young-zebra-sand

Nipah Virus Glycoprotein G
0.79
84.19
--
12.9 kDa
118
id: deep-lynx-cypress

Nipah Virus Glycoprotein G
0.78
82.80
--
12.8 kDa
118
id: shy-kiwi-topaz

Nipah Virus Glycoprotein G
0.72
71.94
--
1.7 kDa
15
id: quiet-heron-crystal

Nipah Virus Glycoprotein G
0.64
80.82
--
14.0 kDa
127
id: dark-otter-ice

Nipah Virus Glycoprotein G
0.35
84.27
--
13.2 kDa
123