Please use this identifier to cite or link to this item: https://repository.udca.edu.co/handle/11158/2398
Title: The role of pi-interactions and hydrogen bonds in fully protective synthetic malaria vaccine development
Authors: Reyes, César
Moreno-Vranich, Armando
Patarroyo, Manuel Elkin
Issue Date: 2017
Series/Report no.: Biochemical and Biophysical Research Communications;Vol. 484, No. 3 Marz., 11 2017 páginas 501-507
Abstract: 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
URI: https://repository.udca.edu.co/handle/11158/2398
Appears in Collections:CCB. Artículos indexados en Scopus

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