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The high immunogenicity induced by modified sporozoites' malarial peptides depends on their phi (?) and psi (?) angles

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Patarroyo, Manuel E.
Bermudez, Adriana
Alba, Martha P.



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The importance of CSP- and STARP-derived ? and ? dihedral angles in mHABP structure was analysed by 1H NMR in the search for molecules which can be included as components of a first-line-of-defence Plasmodium falciparum sporozoite multi-epitope vaccine against the most lethal form of human malaria. Most of the aforementioned dihedral angles were left-hand-like polyproline type II (PPIIL) structures whilst others had right-hand-like ?-helix (?R), thus allowing mHABPS to fit better into MHCII molecules and thereby form an appropriate pMHCII complex and also establish the H-bonds which stabilise such complex and by this means induce an appropriate immune response. This information has great implications for vaccine development, malaria being one of them. © 2012 Elsevier Inc.
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Binding protein , secondary , High activity binding peptide , Major histocompatibility antigen class 2 , Proline , Protozoal protein , Sporozoite threonine and asparagine rich protein , Sporozoite vaccine , Unclassified drug , Alpha helix , Amino acid sequence , Article , Complex formation , Hydrogen bond , Immunogenicity , Plasmodium falciparum , Priority journal , Protein structure , Proton nuclear magnetic resonance , Amino acid sequence , Animals , Antigens , Aotus trivirgatus , Hla-dr beta-chains , Humans , Malaria vaccines , Molecular sequence data , Nuclear magnetic resonance , Peptide fragments , Peptides , Plasmodium falciparum , Protein structure , Protozoan proteins , Sporozoites , Plasmodium falciparum , ? and ? angles , Antimalarial-vaccine , Hladr?* molecules , Plasmodium falciparum , Pre-erythrocyte stage
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