The role of pi-interactions and hydrogen bonds in fully protective synthetic malaria vaccine development

Analysis of our Plasmodium falciparum malaria parasite peptides’ 1H-NMR database in the search for H-bonds and ?-interactions led us to correlate their presence or absence with a peptide's particular immunological behavior. It was concluded that a 26.5 ± 1.5 Å between positions 1 to 9 of the HLA-DR?1* interacting region was necessary for proper docking of 20mer-long peptides and these MHC Class II molecules for full-protective immunity. Presence of intramolecular H-bonds or ?-interactions leading to righ-handed ?-helix or ?-turn conformation in this peptide's region induces different immune responses or none. PPIIL conformation and the absence of any intramolecular interaction thus became the first feature characterising our immune protection-inducing structures as malaria vaccine candidates. © 2017 Elsevier Inc.

• Fecha de publicación: 2017
• Institución: Universidad del Rosario
• Repositorio: Repositorio EdocUR - U. Rosario
• Idioma: eng
• OAI Identifier: oai:repository.urosario.edu.co:10336/23516
• Acceso en línea: https://doi.org/10.1016/j.bbrc.2017.01.077; https://repository.urosario.edu.co/handle/10336/23516
• Palabra clave: HLA DRB1 antigen; Malaria vaccine; HLA antigen class 2; Malaria vaccine; Peptide; Protein binding; Recombinant vaccine; Animal experiment; Animal model; Antibody titer; Aotus; Article; Conformation; Force; Hydrogen bond; Immune response; Immunity; Immunofluorescence; Major histocompatibility complex; Molecular docking; Molecular interaction; Nonhuman; Peptide synthesis; Ph; Pi interaction; Priority journal; Proton nuclear magnetic resonance; Static electricity; Binding site; Chemistry; Drug design; Hydrogen bond; Procedures; Protein analysis; Protein conformation; Sequence analysis; Structure activity relation; Ultrastructure; Binding Sites; Drug Design; Histocompatibility Antigens Class II; HLA-DRB1 Chains; Hydrogen Bonding; Malaria Vaccines; Peptides; Protein Binding; Protein Conformation; Protein Interaction Mapping; Structure-Activity Relationship; Hydrogen bond; Malaria; TCR-peptide-MHC complex; X—H-? interaction; Synthetic; Protein; Sequence Analysis; Vaccines
• License: Abierto (Texto Completo)