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The role of pi-interactions and hydrogen bonds in fully protective synthetic malaria vaccine development
| dc.creator | Reyes C. | spa |
| dc.creator | Moreno-Vranich A. | spa |
| dc.creator | Patarroyo M.E. | spa |
| dc.date.accessioned | 2020-05-26T00:02:42Z | |
| dc.date.available | 2020-05-26T00:02:42Z | |
| dc.date.created | 2017 | spa |
| dc.description.abstract | Analysis of our Plasmodium falciparum malaria parasite peptides’ 1H-NMR database in the search for H-bonds and ?-interactions led us to correlate their presence or absence with a peptide's particular immunological behavior. It was concluded that a 26.5 ± 1.5 Å between positions 1 to 9 of the HLA-DR?1* interacting region was necessary for proper docking of 20mer-long peptides and these MHC Class II molecules for full-protective immunity. Presence of intramolecular H-bonds or ?-interactions leading to righ-handed ?-helix or ?-turn conformation in this peptide's region induces different immune responses or none. PPIIL conformation and the absence of any intramolecular interaction thus became the first feature characterising our immune protection-inducing structures as malaria vaccine candidates. © 2017 Elsevier Inc. | eng |
| dc.format.mimetype | application/pdf | |
| dc.identifier.doi | https://doi.org/10.1016/j.bbrc.2017.01.077 | |
| dc.identifier.issn | 0006291X | |
| dc.identifier.issn | 10902104 | |
| dc.identifier.uri | https://repository.urosario.edu.co/handle/10336/23516 | |
| dc.language.iso | eng | spa |
| dc.publisher | Elsevier B.V. | spa |
| dc.relation.citationEndPage | 507 | |
| dc.relation.citationIssue | No. 3 | |
| dc.relation.citationStartPage | 501 | |
| dc.relation.citationTitle | Biochemical and Biophysical Research Communications | |
| dc.relation.citationVolume | Vol. 484 | |
| dc.relation.ispartof | Biochemical and Biophysical Research Communications, ISSN:0006291X, 10902104, Vol.484, No.3 (2017); pp. 501-507 | spa |
| dc.relation.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85011030545&doi=10.1016%2fj.bbrc.2017.01.077&partnerID=40&md5=55d439795794ba2c0d2eb1624b7bc159 | spa |
| dc.rights.accesRights | info:eu-repo/semantics/openAccess | |
| dc.rights.acceso | Abierto (Texto Completo) | spa |
| dc.source.instname | instname:Universidad del Rosario | spa |
| dc.source.reponame | reponame:Repositorio Institucional EdocUR | spa |
| dc.subject.keyword | HLA DRB1 antigen | spa |
| dc.subject.keyword | Synthetic | eng |
| dc.subject.keyword | HLA antigen class 2 | spa |
| dc.subject.keyword | Malaria vaccine | spa |
| dc.subject.keyword | Peptide | spa |
| dc.subject.keyword | Protein binding | spa |
| dc.subject.keyword | Recombinant vaccine | spa |
| dc.subject.keyword | Animal experiment | spa |
| dc.subject.keyword | Animal model | spa |
| dc.subject.keyword | Antibody titer | spa |
| dc.subject.keyword | Aotus | spa |
| dc.subject.keyword | Article | spa |
| dc.subject.keyword | Conformation | spa |
| dc.subject.keyword | Force | spa |
| dc.subject.keyword | Hydrogen bond | spa |
| dc.subject.keyword | Immune response | spa |
| dc.subject.keyword | Immunity | spa |
| dc.subject.keyword | Immunofluorescence | spa |
| dc.subject.keyword | Major histocompatibility complex | spa |
| dc.subject.keyword | Molecular docking | spa |
| dc.subject.keyword | Molecular interaction | spa |
| dc.subject.keyword | Nonhuman | spa |
| dc.subject.keyword | Peptide synthesis | spa |
| dc.subject.keyword | Ph | spa |
| dc.subject.keyword | Pi interaction | spa |
| dc.subject.keyword | Priority journal | spa |
| dc.subject.keyword | Proton nuclear magnetic resonance | spa |
| dc.subject.keyword | Static electricity | spa |
| dc.subject.keyword | Binding site | spa |
| dc.subject.keyword | Chemistry | spa |
| dc.subject.keyword | Drug design | spa |
| dc.subject.keyword | Hydrogen bond | spa |
| dc.subject.keyword | Procedures | spa |
| dc.subject.keyword | Protein analysis | spa |
| dc.subject.keyword | Protein conformation | spa |
| dc.subject.keyword | Sequence analysis | spa |
| dc.subject.keyword | Structure activity relation | spa |
| dc.subject.keyword | Ultrastructure | spa |
| dc.subject.keyword | Binding Sites | spa |
| dc.subject.keyword | Drug Design | spa |
| dc.subject.keyword | Histocompatibility Antigens Class II | spa |
| dc.subject.keyword | HLA-DRB1 Chains | spa |
| dc.subject.keyword | Hydrogen Bonding | spa |
| dc.subject.keyword | Malaria Vaccines | spa |
| dc.subject.keyword | Peptides | spa |
| dc.subject.keyword | Protein Binding | spa |
| dc.subject.keyword | Protein Conformation | spa |
| dc.subject.keyword | Protein Interaction Mapping | spa |
| dc.subject.keyword | Sequence Analysis | eng |
| dc.subject.keyword | Structure-Activity Relationship | spa |
| dc.subject.keyword | Vaccines | eng |
| dc.subject.keyword | Hydrogen bond | spa |
| dc.subject.keyword | Malaria | spa |
| dc.subject.keyword | TCR-peptide-MHC complex | spa |
| dc.subject.keyword | X—H-? interaction | spa |
| dc.title | The role of pi-interactions and hydrogen bonds in fully protective synthetic malaria vaccine development | spa |
| dc.type | article | eng |
| dc.type.hasVersion | info:eu-repo/semantics/publishedVersion | |
| dc.type.spa | Artículo | spa |



