Ítem
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The role of pi-interactions and hydrogen bonds in fully protective synthetic malaria vaccine development
Título de la revista
Autores
Reyes C.
Moreno-Vranich A.
Patarroyo M.E.
Fecha
2017
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Elsevier B.V.
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Resumen
Abstract
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.
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Keywords
HLA DRB1 antigen , Synthetic , 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 , Sequence Analysis , Structure-Activity Relationship , Vaccines , Hydrogen bond , Malaria , TCR-peptide-MHC complex , X—H-? interaction
