Gauche+ side-chain orientation as a key factor in the search for an immunogenic peptide mixture leading to a complete fully protective vaccine
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 antimalar...
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2014
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Acceso en línea: | https://repository.urosario.edu.co/handle/10336/23461 https://doi.org/10.1016/j.vaccine.2014.02.003 |
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ir-10336-234612022-05-02T12:37:20Z Gauche+ side-chain orientation as a key factor in the search for an immunogenic peptide mixture leading to a complete fully protective vaccine Bermudez, Adriana Calderon, Dayana Moreno-Vranich, Armando Almonacid, Hannia Patarroyo, Manuel A. Poloche, Andrés Patarroyo, Manuel E. Malaria vaccine 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 Amino acid sequence Animals Antibody formation Aotus trivirgatus Binding sites Hla-dr beta-chains Malaria vaccines Molecular sequence data Oligopeptides Protein conformation Antimalarial vaccine Peptide mixtures Protective immunity protozoan falciparum immunologic Adjuvants Antibodies Malaria 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. 2014 2020-05-26T00:02:14Z info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 0264410X 13588745 https://repository.urosario.edu.co/handle/10336/23461 https://doi.org/10.1016/j.vaccine.2014.02.003 eng info:eu-repo/semantics/openAccess application/pdf Elsevier BV instname:Universidad del Rosario |
institution |
EdocUR - Universidad del Rosario |
collection |
DSpace |
language |
Inglés (English) |
topic |
Malaria vaccine 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 Amino acid sequence Animals Antibody formation Aotus trivirgatus Binding sites Hla-dr beta-chains Malaria vaccines Molecular sequence data Oligopeptides Protein conformation Antimalarial vaccine Peptide mixtures Protective immunity protozoan falciparum immunologic Adjuvants Antibodies Malaria |
spellingShingle |
Malaria vaccine 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 Amino acid sequence Animals Antibody formation Aotus trivirgatus Binding sites Hla-dr beta-chains Malaria vaccines Molecular sequence data Oligopeptides Protein conformation Antimalarial vaccine Peptide mixtures Protective immunity protozoan falciparum immunologic Adjuvants Antibodies Malaria Bermudez, Adriana Calderon, Dayana Moreno-Vranich, Armando Almonacid, Hannia Patarroyo, Manuel A. Poloche, Andrés Patarroyo, Manuel E. Gauche+ side-chain orientation as a key factor in the search for an immunogenic peptide mixture leading to a complete fully protective vaccine |
description |
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. |
format |
Artículo (Article) |
author |
Bermudez, Adriana Calderon, Dayana Moreno-Vranich, Armando Almonacid, Hannia Patarroyo, Manuel A. Poloche, Andrés Patarroyo, Manuel E. |
author_facet |
Bermudez, Adriana Calderon, Dayana Moreno-Vranich, Armando Almonacid, Hannia Patarroyo, Manuel A. Poloche, Andrés Patarroyo, Manuel E. |
author_sort |
Bermudez, Adriana |
title |
Gauche+ side-chain orientation as a key factor in the search for an immunogenic peptide mixture leading to a complete fully protective vaccine |
title_short |
Gauche+ side-chain orientation as a key factor in the search for an immunogenic peptide mixture leading to a complete fully protective vaccine |
title_full |
Gauche+ side-chain orientation as a key factor in the search for an immunogenic peptide mixture leading to a complete fully protective vaccine |
title_fullStr |
Gauche+ side-chain orientation as a key factor in the search for an immunogenic peptide mixture leading to a complete fully protective vaccine |
title_full_unstemmed |
Gauche+ side-chain orientation as a key factor in the search for an immunogenic peptide mixture leading to a complete fully protective vaccine |
title_sort |
gauche+ side-chain orientation as a key factor in the search for an immunogenic peptide mixture leading to a complete fully protective vaccine |
publisher |
Elsevier BV |
publishDate |
2014 |
url |
https://repository.urosario.edu.co/handle/10336/23461 https://doi.org/10.1016/j.vaccine.2014.02.003 |
_version_ |
1740172626398019584 |
score |
12,131701 |