In silico directed evolution EvoBind (v2) designs novel peptide binders based only on a protein target sequence. It is not necessary to specify any target residues within the protein sequence or the length of the binder (although this is possible). Cyclic binder design is also possible. EvoBind2 accounts for adaptation of the receptor interface structure to the peptide being designed during optimisation: sequence and structure is generated simultaneously. This consideration of flexibility is crucial for binding. EvoBind is the first protocol that only relies on a protein sequence to design a binder with experimentally verified cyclic design capacity. Li, Q., Vlachos, E.N. & Bryant, P. Design of linear and cyclic peptide binders from protein sequence information. Commun Chem 8, 211 (2025). https://doi.org/10.1038/s42004-025-01601-3
id: misty-wolf-ruby

Nipah Virus Glycoprotein G
0.01
62.05
--
5.7 kDa
50
id: quick-cobra-ruby

Nipah Virus Glycoprotein G
0.82
65.65
--
2.1 kDa
19
id: gentle-cobra-quartz

Nipah Virus Glycoprotein G
0.60
62.64
--
1.8 kDa
15
id: ivory-mole-clay

Nipah Virus Glycoprotein G
0.67
71.52
--
2.2 kDa
18
id: crimson-eagle-opal

Nipah Virus Glycoprotein G
0.03
41.98
--
5.8 kDa
50
id: young-dove-frost

Nipah Virus Glycoprotein G
0.54
73.95
--
2.1 kDa
19
id: hollow-shark-sand

Nipah Virus Glycoprotein G
0.40
52.05
--
9.5 kDa
80
id: violet-vole-moss

Nipah Virus Glycoprotein G
0.72
79.43
--
3.5 kDa
30
id: strong-tiger-frost

Nipah Virus Glycoprotein G
0.71
53.47
--
2.1 kDa
18
id: silver-seal-birch

Nipah Virus Glycoprotein G
0.46
75.92
--
1.8 kDa
15