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.date.accessioned2019-02-08T19:45:56Z
dc.date.available2019-02-08T19:45:56Z
dc.date.created2015
dc.identifier.issnISSN 1932-6203
dc.identifier.urihttp://repository.urosario.edu.co/handle/10336/19030
dc.descriptionDetermining 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.
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.relation.ispartofPLoS ONE, ISSN: 1932-6203, Vol. 10/No. 4 (2015)
dc.relation.urihttps://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0123249&type=printable
dc.rights.uri
dc.subjectBinding Protein
dc.subjectEpitope
dc.subjectHla Dr Antigen
dc.subjectHydrogen
dc.subjectMalaria Vaccine
dc.subjectNitrogen
dc.subjectOxygen
dc.subjectProline
dc.subjectSodium Chloride
dc.subjectSynthetic Peptide
dc.subjectMalaria Vaccine
dc.subjectRecombinant Vaccine
dc.subjectAnimal Experiment
dc.subjectAnimal Model
dc.subjectAntigen Antibody Reaction
dc.subjectAotus
dc.subjectArticle
dc.subjectBinding Site
dc.subjectControlled Study
dc.subjectDrug Structure
dc.subjectElectron
dc.subjectHydrogen Bond
dc.subjectImmune Protection Inducing Protein Structure
dc.subjectImmune Response
dc.subjectImmunoassay
dc.subjectImmunogenicity
dc.subjectMalaria
dc.subjectNonhuman
dc.subjectParasite Virulence
dc.subjectPeptide Synthesis
dc.subjectPhysical Chemistry
dc.subjectPlasmodium Falciparum
dc.subjectProtein Binding
dc.subjectProtein Structure
dc.subjectAnimal
dc.subjectChemistry
dc.subjectHaplorhini
dc.subjectProtein Conformation
dc.subjectAnimals
dc.subjectElectrons
dc.subjectHaplorhini
dc.subjectMalaria Vaccines
dc.subjectProtein Conformation
dc.subjectVaccines, Synthetic
dc.subject.ddc574
dc.subject.lembInmunología
dc.subject.lembProteínas portadoras
dc.subject.lembAntígenos
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 development
dc.typearticle
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.type.spaArtículo
dc.rights.accesoAbierto (Texto Completo)
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
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: 22305225
dc.rights.cchttps://creativecommons.org/licenses/by/4.0/
dc.creator.googlePatarroyo, Manuel Elkin
dc.creator.googleBermudez, Adriana
dc.creator.googleAlba, Martha Patricia
dc.creator.googleVanegas, Magnolia
dc.creator.googleMoreno-Vranich, Armando
dc.creator.googlePoloche, Luis Antonio
dc.creator.googlePatarroyo, Manuel Alfonso


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