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IMPIPS : The Immune Protection-Inducing Protein Structure concept in the search for steric-electron and topochemical principles for complete fully-protective chemically synthesised vaccine development

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dc.creatorPatarroyo, Manuel Elkin
dc.creatorBermudez, Adriana
dc.creatorAlba, Martha Patricia
dc.creatorVanegas, Magnolia
dc.creatorMoreno-Vranich, Armando
dc.creatorPoloche, Luis Antonio
dc.creatorPatarroyo, Manuel A.
dc.creator.googlePatarroyo, Manuel Elkinspa
dc.creator.googleBermudez, Adrianaspa
dc.creator.googleAlba, Martha Patriciaspa
dc.creator.googleVanegas, Magnoliaspa
dc.creator.googleMoreno-Vranich, Armandospa
dc.creator.googlePoloche, Luis Antoniospa
dc.creator.googlePatarroyo, Manuel Alfonsospa
dc.date.accessioned2019-02-08T19:45:56Z
dc.date.available2019-02-08T19:45:56Z
dc.date.created2015
dc.date.issued2015-04-16
dc.description.abstractDetermining immune protection-inducing protein structures (IMPIPS) involves defining the stereo-electron and topochemical characteristics which are essential in MHC-p-TCR complex formation. Modified high activity binding peptides (mHABP) were thus synthesised to produce a large panel of IMPIPS measuring 26.5 ±3.5Å between the farthest atoms fitting into Pockets 1 to 9 of HLA-DRβ1∗structures. They displayed a polyproline II-like (PPIIL) structure with their backbone O and N atoms orientated to establish H-bonds with specific residues from HLA-DRβ∗-peptide binding regions (PBR). Residues having specific charge and gauche+ orientation regarding p3χ1, p5χ2, and p7χ1 angles determined appropriate rotamer orientation for perfectly fitting into the TCR to induce an appropriate immune response. Immunological assays in Aotus monkeys involving IMPIPS mixtures led to promising results; taken together with the aforementioned physicochemical principles, noninterfering, long-lasting, protection-inducing, multi-epitope, multistage, minimal subunit-based chemically-synthesised peptides can be designed against diseases scourging humankind. © 2015 Patarroyo et al.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0123249
dc.identifier.issn1932-6203
dc.identifier.urihttp://repository.urosario.edu.co/handle/10336/19030
dc.language.isoengspa
dc.relation.citationIssueNo. 4
dc.relation.citationTitlePLoS ONE
dc.relation.citationVolumeVol. 10
dc.relation.ispartofPLoS ONE, ISSN: 1932-6203, Vol. 10/No. 4 (2015)spa
dc.relation.urihttps://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0123249&type=printablespa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.rights.cchttps://creativecommons.org/licenses/by/4.0/spa
dc.source.bibliographicCitationMurray, C.J., Rosenfeld, L.C., Lim, S.S., Andrews, K.G., Foreman, K.J., Haring, D., Global malaria mortality between 1980 and 2010: A systematic analysis (2012) Lancet, 379, pp. 413-431. , PMID: 22305225spa
dc.source.instnameinstname:Universidad del Rosario
dc.source.reponamereponame:Repositorio Institucional EdocUR
dc.subjectProteína de uniónspa
dc.subjectepítopospa
dc.subjectAntígeno Hla Drspa
dc.subjectHidrógenospa
dc.subjectVacuna contra la malariaspa
dc.subjectNitrógenospa
dc.subjectOxígenospa
dc.subjectProlinaspa
dc.subjectCloruro de sodiospa
dc.subjectPéptido sintéticospa
dc.subjectVacuna recombinantespa
dc.subjectAnimal Experimentspa
dc.subjectModelo animalspa
dc.subjectReacción de anticuerpo de antígenospa
dc.subjectAotospa
dc.subjectSitio de uniónspa
dc.subjectEstudio controladospa
dc.subjectEstructura de la drogaspa
dc.subjectElectrónspa
dc.subjectEnlace de hidrógenospa
dc.subjectEstructura proteica inductora de protección inmunitariaspa
dc.subjectRespuesta inmunespa
dc.subjectinmunoensayospa
dc.subjectinmunogenicidadspa
dc.subjectMalariaspa
dc.subjectNo humanospa
dc.subjectVirulencia del parásitospa
dc.subjectSíntesis de péptidosspa
dc.subjectQuímica Físicaspa
dc.subjectPlasmodium falciparumspa
dc.subjectEnlace proteicospa
dc.subjectEstructura de la proteínaspa
dc.subjectAnimalspa
dc.subjectChemistryspa
dc.subjectHaplorhinspa
dc.subjectConformación de proteínasspa
dc.subject.ddcBiologíaspa
dc.subject.keywordSyntheticeng
dc.subject.keywordNitrogenspa
dc.subject.keywordVaccineseng
dc.subject.keywordProlineeng
dc.subject.keywordSynthetic Peptideeng
dc.subject.keywordSodium Chlorideeng
dc.subject.keywordRecombinant Vaccineeng
dc.subject.keywordAnimal Modeleng
dc.subject.keywordAnimal Experimenteng
dc.subject.keywordAntigen Antibody Reactioneng
dc.subject.keywordAotuseng
dc.subject.keywordBinding Siteeng
dc.subject.keywordControlled Studyeng
dc.subject.keywordDrug Structureeng
dc.subject.keywordElectroneng
dc.subject.keywordHydrogen Bondeng
dc.subject.keywordImmune Protection Inducing Proteineng
dc.subject.keywordStructureeng
dc.subject.keywordImmune Responseeng
dc.subject.keywordImmunoassayeng
dc.subject.keywordBinding Proteineng
dc.subject.keywordEpitopeeng
dc.subject.keywordHla Dr Antigeneng
dc.subject.keywordHydrogeneng
dc.subject.keywordMalaria Vaccineeng
dc.subject.keywordOxygeneng
dc.subject.keywordImmunogenicityeng
dc.subject.keywordNonhumaneng
dc.subject.keywordParasite Virulenceeng
dc.subject.keywordPeptide Synthesiseng
dc.subject.keywordPhysical Chemistryeng
dc.subject.keywordPlasmodium Falciparumeng
dc.subject.keywordProtein Bindingeng
dc.subject.keywordProtein Structureeng
dc.subject.keywordChemistryeng
dc.subject.keywordProtein Conformationeng
dc.subject.keywordHaplorhinieng
dc.subject.keywordAnimalseng
dc.subject.keywordElectronseng
dc.subject.lembInmunologíaspa
dc.subject.lembProteínas portadorasspa
dc.subject.lembAntígenosspa
dc.titleIMPIPS : The Immune Protection-Inducing Protein Structure concept in the search for steric-electron and topochemical principles for complete fully-protective chemically synthesised vaccine developmentspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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