Affilin® libraries have been generated to a complexity of 1019
All Affilin® molecules are based on the human protein Ubiquitin. Ubiquitin naturally interacts with numerous other proteins but does not show high affinity binding activities towards any of these proteins.
Scil Proteins has modelled and tested several binding patches on Ubiquitin by randomizing surface exposed amino acid residues. This work finally led to the generation of two highly diverse libraries.
The Affilin® monomer library contains variants with eight randomized amino acid positions. Nineteen natural amino acids are allowed on each randomized position, leading to a library complexity of 1.7 x 1010 individual proteins. In Affilin® dimer libraries, 14 amino acid positions are randomized generating a complexity of ~ up to 1019.
