Design and functional characterization of Salmo salar TLR5 agonist peptides derived from High Mobility Group B1 acidic tail.

<p>Based on the structural knowledge of TLR5 surface using blind docking platforms, a series of peptides derived from HMGB1 truncated acidic tail from Salmo salar was designed TLR5 agonistic. Also, a template peptide with the wild type C-terminal acidic tail sequence as reference was included (SsOri). Peptide binding poses complexed on TLR5 ectodomain model from each algorithm were filtrated based on docking scoring functions and predicted theoretical binding affinity of complex.</p>