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Antiviral lipopeptide-cell membrane Interaction Is Influenced by PEG linker length

dc.contributor.authorAugusto, Marcelo T.
dc.contributor.authorHollmann, Axel
dc.contributor.authorPorotto, Matteo
dc.contributor.authorMoscona, Anne
dc.contributor.authorSantos, Nuno C.
dc.date.accessioned2018-05-25T14:55:18Z
dc.date.available2018-05-25T14:55:18Z
dc.date.issued2017
dc.description© 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/)pt_PT
dc.description.abstractA 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.pt_PT
dc.description.sponsorshipThis work was supported by Fundação para a Ciência e a Tecnologia – Ministério da Ciência, Tecnologia e Ensino Superior (FCT-MCTES, Portugal) grant PTDC/BBB-BQB/3494/2014, and by NIH grants RO1AI114736, R33AI101333 and RO1AI031971 to A.M. M.T.A. also acknowledges FCT-MCTES fellowship SFRH/BD/95624/2013 and Fundação Luso-Americana para o Desenvolvimento (FLAD) project 4/2016.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationMolecules 2017, 22, 1190pt_PT
dc.identifier.doi10.3390/molecules22071190pt_PT
dc.identifier.issn1420-3049
dc.identifier.urihttp://hdl.handle.net/10451/33662
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherMDPIpt_PT
dc.relationBroad-spectrum antiviral peptides against respiratory viruses
dc.relationBROAD-SPECTRUM FUSION INHIBITORS AGAINST ENVELOPED VIRUSES
dc.relation.publisherversionhttp://www.mdpi.com/journal/moleculespt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectAntiviralpt_PT
dc.subjectCholesterolpt_PT
dc.subjectMembranespt_PT
dc.subjectParamyxovirusespt_PT
dc.subjectPeptidespt_PT
dc.titleAntiviral lipopeptide-cell membrane Interaction Is Influenced by PEG linker lengthpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleBroad-spectrum antiviral peptides against respiratory viruses
oaire.awardTitleBROAD-SPECTRUM FUSION INHIBITORS AGAINST ENVELOPED VIRUSES
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBBB-BQB%2F3494%2F2014/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/OE/SFRH%2FBD%2F95624%2F2013/PT
oaire.citation.issue7pt_PT
oaire.citation.startPagepii: E1190pt_PT
oaire.citation.titleMoleculespt_PT
oaire.citation.volume22pt_PT
oaire.fundingStream3599-PPCDT
oaire.fundingStreamOE
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isProjectOfPublication62b1fcf5-31a2-48aa-ad0c-a877afd7744e
relation.isProjectOfPublicationc2f9d622-939c-43d2-9002-f5680cd56f6f
relation.isProjectOfPublication.latestForDiscovery62b1fcf5-31a2-48aa-ad0c-a877afd7744e

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