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dc.creatorAugusto, Marcelo T.-
dc.creatorHollmann, Axel-
dc.creatorPorotto, Matteo-
dc.creatorMoscona, Anne-
dc.creatorSantos, Nuno C.-
dc.date2018-04-05T17:16:32Z-
dc.date2018-04-05T17:16:32Z-
dc.date2017-07-
dc.date2018-04-05T13:43:42Z-
dc.date.accessioned2019-04-29T15:55:53Z-
dc.date.available2019-04-29T15:55:53Z-
dc.identifierAugusto, Marcelo T.; Hollmann, Axel; Porotto, Matteo; Moscona, Anne; Santos, Nuno C.; Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length; Molecular Diversity Preservation International; Molecules; 22; 7; 7-2017-
dc.identifier1420-3049-
dc.identifierhttp://hdl.handle.net/11336/40899-
dc.identifierCONICET Digital-
dc.identifierCONICET-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/305616-
dc.descriptionA set of lipopeptides was recently reported for their broad-spectrum antiviral activity against viruses belonging to the Paramyxoviridae family, including human parainfluenza virus type 3 and Nipah virus. Among them, the peptide with a 24-unit PEG linker connecting it to a cholesterol moiety (VG-PEG24-Chol) was found to be the best membrane fusion inhibitory peptide. Here, we evaluated the interaction of the same set of peptides with biomembrane model systems and isolated human peripheral blood mononuclear cells (PBMC). VG-PEG24-Chol showed the highest insertion rate and it was among the peptides that induced a larger change on the surface pressure of cholesterol rich membranes. This peptide also displayed a high affinity towards PBMC membranes. These data provide new information about the dynamics of peptide-membrane interactions of a specific group of antiviral peptides, known for their potential as multipotent paramyxovirus antivirals.-
dc.descriptionFil: Augusto, Marcelo T.. Universidade de Lisboa. Instituto de Medicina Molecular; Portugal-
dc.descriptionFil: Hollmann, Axel. Universidade de Lisboa. Instituto de Medicina Molecular; Portugal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina. Universidad Nacional de Quilmes; Argentina-
dc.descriptionFil: Porotto, Matteo. Columbia University Medical Center; Estados Unidos-
dc.descriptionFil: Moscona, Anne. Columbia University Medical Center; Estados Unidos-
dc.descriptionFil: Santos, Nuno C.. Universidade de Lisboa. Instituto de Medicina Molecular; Portugal-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherMolecular Diversity Preservation International-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/1420-3049/22/7/1190-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3390/molecules22071190-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightshttps://creativecommons.org/licenses/by/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.subjectPARAMYXOVIRUSES-
dc.subjectPEPTIDES-
dc.subjectANTIVIRAL-
dc.subjectCHOLESTEROL-
dc.subjectMEMBRANES-
dc.subjectOtras Ciencias Biológicas-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleAntiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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