The role of pi-interactions and hydrogen bonds in fully protective synthetic malaria vaccine development
Artículo de revista
2017
Analysis of ourPlasmodium falciparummalaria parasite peptides'1H-NMR database in the search for H-bonds andp-interactions led us to correlate their presence or absence with a peptide's particularimmunological behavior. It was concluded that a 26.5±1.5 Å between positions 1 to 9 of the HLA-DRb1*interacting region was necessary for proper docking of 20mer-long peptides and these MHC Class IImolecules for full-protective immunity. Presence of intramolecular H-bonds orp-interactions leading torigh-handeda-helix orb-turn conformation in this peptide's region induces different immune responsesor none. PPIILconformation and the absence of any intramolecular interaction thus became thefirstfeature characterising our immune protection-inducing structures as malaria vaccine candidates
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Título: 1-s2.0-S0006291X17301286-main.pdf
Tamaño: 2.159Mb
PDF
Título: 1-s2.0-S0006291X17301286-main.pdf
Tamaño: 2.159Mb

