Towards a poly-functional synthetic-antimalarial vaccine: Incorporating non-natural elements into artificially-made peptides for mimicking functional pathogen ligand structures representing new site-directed vaccine components

The molecular basis for obtaining novel anti-malarial vaccine candidates depends on a considered selection of antigenic peptides, mainly derived from Plasmodium antigens' non-polymorphic regions. Since such targeted-molecules are poorly immunogenic when tested as vaccine components, they usuall...

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Tipo de recurso:
Fecha de publicación:
2013
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/23810
Acceso en línea:
https://doi.org/10.2174/1573395510666140401180738
https://repository.urosario.edu.co/handle/10336/23810
Palabra clave:
Amide pseudopeptide
Epitope
Malaria vaccine
Merozoite surface protein 2
Parasite antibody
Peptide vaccine
Peptidomimetic agent
Pseudopeptide
Synthetic peptide
Unclassified drug
Antimalarial activity
Article
Erythrocyte
Human
Immune response
Immunogenicity
Immunoprophylaxis
In vitro study
Malaria
Malaria falciparum
Nonhuman
Parasitemia
Passive immunization
Phase transition
Plasmodium (life cycle stage)
Plasmodium falciparum
Priority journal
Protein binding
Protein hydrolysis
Protein motif
Protein targeting
Public health problem
Rodent malaria
Vaccine production
Antimalarial vaccine
Catalytic antibody
Passive immunisation
Peptide-bond isostere
Peptido-mimetic
Pseudopeptide
Rights
License
Abierto (Texto Completo)
id EDOCUR2_b86fff8fade017d661d8d9179296cb0e
oai_identifier_str oai:repository.urosario.edu.co:10336/23810
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling 42a1d1c8-859d-41fb-bd07-781512f8b10c-176e03223-040d-4e46-864f-3bdecc8d2790-12020-05-26T00:05:37Z2020-05-26T00:05:37Z2013The molecular basis for obtaining novel anti-malarial vaccine candidates depends on a considered selection of antigenic peptides, mainly derived from Plasmodium antigens' non-polymorphic regions. Since such targeted-molecules are poorly immunogenic when tested as vaccine components, they usually have to be modified to overcome their immunological phenotype. Transition state theory, explaining how peptidases catalyse a given peptide bond breakage, thus led to reduced amide pseudopeptides being proposed as possible mimetics for a transition-state. Stabilising such high-energy molecular stages could become a strategy for inducing antibodies potentially harbouring catalytic properties. Hence, isostere-bond peptido-mimetics represented a rational choice as potential abzyme-inducers and site-directed designed reduced amide pseudopeptides for obtaining peptide-analogues from selected malarial high-binding motifs. This novel family of vaccine candidates has proved to be an efficient functional antibody-inducer, the latter acting as efficient blockers of Plasmodium infection of human and mouse RBCs. © 2013 Bentham Science Publishers.application/pdfhttps://doi.org/10.2174/157339551066614040118073815733955https://repository.urosario.edu.co/handle/10336/23810engBentham Science Publishers B.V.275No. 4261Current Immunology ReviewsVol. 9Current Immunology Reviews, ISSN:15733955, Vol.9, No.4 (2013); pp. 261-275https://www.scopus.com/inward/record.uri?eid=2-s2.0-84900810092&doi=10.2174%2f1573395510666140401180738&partnerID=40&md5=1996fa48a6b02b66616178dfe32576b8Abierto (Texto Completo)http://purl.org/coar/access_right/c_abf2instname:Universidad del Rosarioreponame:Repositorio Institucional EdocURAmide pseudopeptideEpitopeMalaria vaccineMerozoite surface protein 2Parasite antibodyPeptide vaccinePeptidomimetic agentPseudopeptideSynthetic peptideUnclassified drugAntimalarial activityArticleErythrocyteHumanImmune responseImmunogenicityImmunoprophylaxisIn vitro studyMalariaMalaria falciparumNonhumanParasitemiaPassive immunizationPhase transitionPlasmodium (life cycle stage)Plasmodium falciparumPriority journalProtein bindingProtein hydrolysisProtein motifProtein targetingPublic health problemRodent malariaVaccine productionAntimalarial vaccineCatalytic antibodyPassive immunisationPeptide-bond isosterePeptido-mimeticPseudopeptideTowards a poly-functional synthetic-antimalarial vaccine: Incorporating non-natural elements into artificially-made peptides for mimicking functional pathogen ligand structures representing new site-directed vaccine componentsarticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Lozano J.M.Patarroyo M.E.10336/23810oai:repository.urosario.edu.co:10336/238102022-05-02 07:37:14.811286https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv Towards a poly-functional synthetic-antimalarial vaccine: Incorporating non-natural elements into artificially-made peptides for mimicking functional pathogen ligand structures representing new site-directed vaccine components
title Towards a poly-functional synthetic-antimalarial vaccine: Incorporating non-natural elements into artificially-made peptides for mimicking functional pathogen ligand structures representing new site-directed vaccine components
spellingShingle Towards a poly-functional synthetic-antimalarial vaccine: Incorporating non-natural elements into artificially-made peptides for mimicking functional pathogen ligand structures representing new site-directed vaccine components
Amide pseudopeptide
Epitope
Malaria vaccine
Merozoite surface protein 2
Parasite antibody
Peptide vaccine
Peptidomimetic agent
Pseudopeptide
Synthetic peptide
Unclassified drug
Antimalarial activity
Article
Erythrocyte
Human
Immune response
Immunogenicity
Immunoprophylaxis
In vitro study
Malaria
Malaria falciparum
Nonhuman
Parasitemia
Passive immunization
Phase transition
Plasmodium (life cycle stage)
Plasmodium falciparum
Priority journal
Protein binding
Protein hydrolysis
Protein motif
Protein targeting
Public health problem
Rodent malaria
Vaccine production
Antimalarial vaccine
Catalytic antibody
Passive immunisation
Peptide-bond isostere
Peptido-mimetic
Pseudopeptide
title_short Towards a poly-functional synthetic-antimalarial vaccine: Incorporating non-natural elements into artificially-made peptides for mimicking functional pathogen ligand structures representing new site-directed vaccine components
title_full Towards a poly-functional synthetic-antimalarial vaccine: Incorporating non-natural elements into artificially-made peptides for mimicking functional pathogen ligand structures representing new site-directed vaccine components
title_fullStr Towards a poly-functional synthetic-antimalarial vaccine: Incorporating non-natural elements into artificially-made peptides for mimicking functional pathogen ligand structures representing new site-directed vaccine components
title_full_unstemmed Towards a poly-functional synthetic-antimalarial vaccine: Incorporating non-natural elements into artificially-made peptides for mimicking functional pathogen ligand structures representing new site-directed vaccine components
title_sort Towards a poly-functional synthetic-antimalarial vaccine: Incorporating non-natural elements into artificially-made peptides for mimicking functional pathogen ligand structures representing new site-directed vaccine components
dc.subject.keyword.spa.fl_str_mv Amide pseudopeptide
Epitope
Malaria vaccine
Merozoite surface protein 2
Parasite antibody
Peptide vaccine
Peptidomimetic agent
Pseudopeptide
Synthetic peptide
Unclassified drug
Antimalarial activity
Article
Erythrocyte
Human
Immune response
Immunogenicity
Immunoprophylaxis
In vitro study
Malaria
Malaria falciparum
Nonhuman
Parasitemia
Passive immunization
Phase transition
Plasmodium (life cycle stage)
Plasmodium falciparum
Priority journal
Protein binding
Protein hydrolysis
Protein motif
Protein targeting
Public health problem
Rodent malaria
Vaccine production
Antimalarial vaccine
Catalytic antibody
Passive immunisation
Peptide-bond isostere
Peptido-mimetic
Pseudopeptide
topic Amide pseudopeptide
Epitope
Malaria vaccine
Merozoite surface protein 2
Parasite antibody
Peptide vaccine
Peptidomimetic agent
Pseudopeptide
Synthetic peptide
Unclassified drug
Antimalarial activity
Article
Erythrocyte
Human
Immune response
Immunogenicity
Immunoprophylaxis
In vitro study
Malaria
Malaria falciparum
Nonhuman
Parasitemia
Passive immunization
Phase transition
Plasmodium (life cycle stage)
Plasmodium falciparum
Priority journal
Protein binding
Protein hydrolysis
Protein motif
Protein targeting
Public health problem
Rodent malaria
Vaccine production
Antimalarial vaccine
Catalytic antibody
Passive immunisation
Peptide-bond isostere
Peptido-mimetic
Pseudopeptide
description The molecular basis for obtaining novel anti-malarial vaccine candidates depends on a considered selection of antigenic peptides, mainly derived from Plasmodium antigens' non-polymorphic regions. Since such targeted-molecules are poorly immunogenic when tested as vaccine components, they usually have to be modified to overcome their immunological phenotype. Transition state theory, explaining how peptidases catalyse a given peptide bond breakage, thus led to reduced amide pseudopeptides being proposed as possible mimetics for a transition-state. Stabilising such high-energy molecular stages could become a strategy for inducing antibodies potentially harbouring catalytic properties. Hence, isostere-bond peptido-mimetics represented a rational choice as potential abzyme-inducers and site-directed designed reduced amide pseudopeptides for obtaining peptide-analogues from selected malarial high-binding motifs. This novel family of vaccine candidates has proved to be an efficient functional antibody-inducer, the latter acting as efficient blockers of Plasmodium infection of human and mouse RBCs. © 2013 Bentham Science Publishers.
publishDate 2013
dc.date.created.spa.fl_str_mv 2013
dc.date.accessioned.none.fl_str_mv 2020-05-26T00:05:37Z
dc.date.available.none.fl_str_mv 2020-05-26T00:05:37Z
dc.type.eng.fl_str_mv article
dc.type.coarversion.fl_str_mv http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.coar.fl_str_mv http://purl.org/coar/resource_type/c_6501
dc.type.spa.spa.fl_str_mv Artículo
dc.identifier.doi.none.fl_str_mv https://doi.org/10.2174/1573395510666140401180738
dc.identifier.issn.none.fl_str_mv 15733955
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/23810
url https://doi.org/10.2174/1573395510666140401180738
https://repository.urosario.edu.co/handle/10336/23810
identifier_str_mv 15733955
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 275
dc.relation.citationIssue.none.fl_str_mv No. 4
dc.relation.citationStartPage.none.fl_str_mv 261
dc.relation.citationTitle.none.fl_str_mv Current Immunology Reviews
dc.relation.citationVolume.none.fl_str_mv Vol. 9
dc.relation.ispartof.spa.fl_str_mv Current Immunology Reviews, ISSN:15733955, Vol.9, No.4 (2013); pp. 261-275
dc.relation.uri.spa.fl_str_mv https://www.scopus.com/inward/record.uri?eid=2-s2.0-84900810092&doi=10.2174%2f1573395510666140401180738&partnerID=40&md5=1996fa48a6b02b66616178dfe32576b8
dc.rights.coar.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.rights.acceso.spa.fl_str_mv Abierto (Texto Completo)
rights_invalid_str_mv Abierto (Texto Completo)
http://purl.org/coar/access_right/c_abf2
dc.format.mimetype.none.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Bentham Science Publishers B.V.
institution Universidad del Rosario
dc.source.instname.spa.fl_str_mv instname:Universidad del Rosario
dc.source.reponame.spa.fl_str_mv reponame:Repositorio Institucional EdocUR
repository.name.fl_str_mv Repositorio institucional EdocUR
repository.mail.fl_str_mv edocur@urosario.edu.co
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