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Conserved binding regions provide the clue for peptide-based vaccine development: A chemical perspective

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dc.creatorCurtidor, Hernando
dc.creatorReyes, Césarspa
dc.creatorBermudez, Adriana
dc.creatorVanegas, Magnoliaspa
dc.creatorVarela, Yahsonspa
dc.creatorPatarroyo, Manuel Espa
dc.date.accessioned2020-05-25T23:57:12Z
dc.date.available2020-05-25T23:57:12Z
dc.date.created2017spa
dc.description.abstractSynthetic peptides have become invaluable biomedical research and medicinal chemistry tools for studying functional roles, i.e., binding or proteolytic activity, naturally-occurring regions' immunogenicity in proteins and developing therapeutic agents and vaccines. Synthetic peptides can mimic protein sites; their structure and function can be easily modulated by specific amino acid replacement. They have major advantages, i.e., they are cheap, easily-produced and chemically stable, lack infectious and secondary adverse reactions and can induce immune responses via T- and B-cell epitopes. Our group has previously shown that using synthetic peptides and adopting a functional approach has led to identifying Plasmodium falciparum conserved regions binding to host cells. Conserved high activity binding peptides' (cHABPs) physicochemical, structural and immunological characteristics have been taken into account for properly modifying and converting them into highly immunogenic, protection-inducing peptides (mHABPs) in the experimental Aotus monkey model. This article describes stereo-electron and topochemical characteristics regarding major histocompatibility complex (MHC)-mHABP-T-cell receptor (TCR) complex formation. Some mHABPs in this complex inducing long-lasting, protective immunity have been named immune protection-inducing protein structures (IMPIPS), forming the subunit components in chemically synthesized vaccines. This manuscript summarizes this particular field and adds our recent findings concerning intramolecular interactions (H-bonds or-interactions) enabling proper IMPIPS structure as well as the peripheral flanking residues (PFR) to stabilize the MHCII-IMPIPS-TCR interaction, aimed at inducing long-lasting, protective immunological memory. © 2017 by the authors. Licensee MDPI, Basel, Switzerland.1.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.3390/molecules22122199
dc.identifier.issn14203049
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/22627
dc.language.isoengspa
dc.publisherMDPI AGspa
dc.relation.citationIssueNo. 12
dc.relation.citationTitleMolecules
dc.relation.citationVolumeVol. 22
dc.relation.ispartofMolecules, ISSN:14203049, Vol.22, No.12 (2017)spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85040339126&doi=10.3390%2fmolecules22122199&partnerID=40&md5=373940215409d243945dd06b138854f4spa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.source.instnameinstname:Universidad del Rosariospa
dc.source.reponamereponame:Repositorio Institucional EdocURspa
dc.subject.keywordLymphocyte antigen receptorspa
dc.subject.keywordMalaria vaccinespa
dc.subject.keywordPeptidespa
dc.subject.keywordProtein bindingspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAnimalspa
dc.subject.keywordBinding sitespa
dc.subject.keywordChemistryspa
dc.subject.keywordHaplorhinispa
dc.subject.keywordHumanspa
dc.subject.keywordImmunologyspa
dc.subject.keywordMajor histocompatibility complexspa
dc.subject.keywordMetabolismspa
dc.subject.keywordMolecular modelspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein conformationspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAnimalsspa
dc.subject.keywordBinding sitesspa
dc.subject.keywordHaplorhinispa
dc.subject.keywordHumansspa
dc.subject.keywordMajor histocompatibility complexspa
dc.subject.keywordMalaria vaccinesspa
dc.subject.keywordModelseng
dc.subject.keywordPeptidesspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordProtein bindingspa
dc.subject.keywordProtein conformationspa
dc.subject.keywordReceptorseng
dc.subject.keywordImmunogenicityspa
dc.subject.keywordMalaria vaccinespa
dc.subject.keywordStructurespa
dc.subject.keywordSynthetic peptidesspa
dc.subject.keywordTherapeuticsspa
dc.titleConserved binding regions provide the clue for peptide-based vaccine development: A chemical perspectivespa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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