A broadly neutralizing antibody was optimized into a nanobody using RFDiffusion before ESMfold-suggested mutations were incorporated into designs. Favorable candidates were further modified through rational design where the binding region with the glycoprotein was optimized. Rationally designed candidates were validated using ESMfold, AlphaFold 2 and AlphaFold 3 before submission, ensuring that all candidates had average pTM, pLDDT, and iPTM >80 while possessing favorable PAE.
id: quick-cat-iron

Nipah Virus Glycoprotein G
Strong
7.2e-8 M
True
27.2 kDa
250
id: rough-bison-maple

Nipah Virus Glycoprotein G
Strong
7.2e-10 M
True
26.6 kDa
249
id: violet-jaguar-rose

Nipah Virus Glycoprotein G
0.32
82.10
--
27.1 kDa
250
id: ivory-bear-orchid

Nipah Virus Glycoprotein G
0.30
82.17
--
27.1 kDa
249
id: strong-moth-topaz

Nipah Virus Glycoprotein G
0.00
80.93
--
27.1 kDa
250
id: soft-bee-frost

Nipah Virus Glycoprotein G
0.63
83.11
--
27.0 kDa
249
id: young-deer-marble

Nipah Virus Glycoprotein G
0.17
84.39
--
27.0 kDa
249
id: lunar-cat-maple

Nipah Virus Glycoprotein G
0.01
82.25
--
27.0 kDa
249
id: shy-ox-vine

Nipah Virus Glycoprotein G
0.00
80.45
--
26.9 kDa
249