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Gauche+ side-chain orientation as a key factor in the search for an immunogenic peptide mixture leading to a complete fully protective vaccine
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Bermudez, Adriana
Calderon, Dayana
Moreno-Vranich, Armando
Almonacid, Hannia
Patarroyo, Manuel A.
Poloche, Andrés
Patarroyo, Manuel E.
Fecha
2014
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Elsevier BV
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Abstract
Topological and stereo-electron characteristics are essential in major histocompability class II-peptide-T-cell receptor (MHC-p-TCR) complex formation for inducing an appropriate immune response. Modified high activity binding peptides (mHABPs) were synthesised for complete full protection antimalarial vaccine development producing a large panel of individually fully protection-inducing protein structures (FPIPS) and very high long-lasting antibody-inducing (VHLLAI) mHABPs. Most of those which did not interfere, compete, inhibit or suppress their individual VHLLAI or FPIPS activity contained or displayed a polyproline II-like (PPIIL) structure when mixed. Here we show that amino acid side-chains located in peptide binding region (PBR) positions p3 and p7 displayed specific electron charges and side-chain gauche+ orientation for interacting with the TCR. Based on the above, and previously described physicochemical principles, non-interfering, long-lasting, full protection-inducing, multi-epitope, multistage, minimal subunit-based chemically synthesised mHABP mixtures can be designed for developing vaccines against diseases scourging humankind, malaria being one of them. © 2014 Elsevier Ltd.
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Keywords
protozoan , Peptide vaccine , Unclassified drug , Very high long lasting antibody inducing modified high activity binding peptide , Animal experiment , Antibody production , Antibody titer , Aotus , Article , Controlled study , Drug mixture , Enzyme linked immunosorbent assay , Gauche side chain orientation , Genotype , Immune response , Immunofluorescence , Immunogenicity , Nonhuman , Priority journal , Protection , Protein structure , Proton nuclear magnetic resonance , Sporozoite , Vaccination , Western blotting , Antimalarial vaccine , Gauche(+) , Peptide mixtures , Protective immunity , ?(1) angle , Adjuvants , Amino acid sequence , Animals , Antibodies , Antibody formation , Aotus trivirgatus , Binding sites , Hla-dr beta-chains , Malaria vaccines , Malaria , Molecular sequence data , Oligopeptides , Protein conformation , Antimalarial vaccine , Peptide mixtures , Protective immunity
