Modifying the acidic tail of High Mobility Group B1 for designing Salmo salar TLR5 agonist peptides

Autor: Vásquez-Suárez, Aleikar, Muñoz-Flores, Carolina, Roa, Francisco, Castillo, Carolina, Romero, Alex, Parra, Natalie, Sandoval, Felipe, Macaya, Luis, Gutiérrez, Nicolás, González, Iván, Lamazares, Emilio, Astuya, Allison, Starck, María Francisca, Ortega, Leonardo, Villegas, Milton F., Agurto, Niza, Montesino, Raquel, Sánchez, Oliberto, Valenzuela, Ariel, Toledo, Jorge R., Acosta, Jannel
Jazyk: angličtina
Rok vydání: 2023
DOI: 10.5281/zenodo.8039986
Popis: 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.
Databáze: OpenAIRE