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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Autores Principales: Bermudez, Adriana, Calderon, Dayana, Moreno-Vranich, Armando, Almonacid, Hannia, Patarroyo, Manuel A., Poloche, Andrés, Patarroyo, Manuel E.
Formato: Artículo (Article)
Lenguaje:Inglés (English)
Publicado: Elsevier BV 2014
Materias:
Acceso en línea:https://repository.urosario.edu.co/handle/10336/23461
https://doi.org/10.1016/j.vaccine.2014.02.003
id ir-10336-23461
recordtype dspace
spelling 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
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