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Effective in vivo targeting of influenza virus through a cell-penetrating/fusion inhibitor tandem peptide anchored to the plasma membrane

2018Journal article Restricted access
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dc.contributor.authorFigueira, Tiago Nascimento
dc.contributor.authorAugusto, Marcelo Tavares
dc.contributor.authorRybkina, K.
dc.contributor.authorStelitano, D.
dc.contributor.authorNoval, M. G.
dc.contributor.authorHarder, O. E.
dc.contributor.authorVeiga, Ana Salome
dc.contributor.authorHuey, D.
dc.contributor.authorAlabi, C. A.
dc.contributor.authorBiswas, S.
dc.contributor.authorNiewiesk, S.
dc.contributor.authorMoscona, A.
dc.contributor.authorSantos, Nuno C.
dc.contributor.authorCastanho, Miguel A. R. B.
dc.contributor.authorPorotto, M.
dc.date.accessioned2019-03-22T12:28:57Z
dc.date.available2019-03-22T12:28:57Z
dc.date.issued2018
dc.description© 2018 American Chemical Societypt_PT
dc.description.abstractThe impact of influenza virus infection is felt each year on a global scale when approximately 5−10% of adults and 20−30% of children globally are infected. While vaccination is the primary strategy for influenza prevention, there are a number of likely scenarios for which vaccination is inadequate, making the development of effective antiviral agents of utmost importance. Anti-influenza treatments with innovative mechanisms of action are critical in the face of emerging viral resistance to the existing drugs. These new antiviral agents are urgently needed to address future epidemic (or pandemic) influenza and are critical for the immune-compromised cohort who cannot be vaccinated. We have previously shown that lipid tagged peptides derived from the C-terminal region of influenza hemagglutinin (HA) were effective influenza fusion inhibitors. In this study, we modified the influenza fusion inhibitors by adding a cell penetrating peptide sequence to promote intracellular targeting. These fusion-inhibiting peptides self-assemble into ∼15−30 nm nanoparticles (NPs), target relevant infectious tissues in vivo, and reduce viral infectivity upon interaction with the cell membrane. Overall, our data show that the CPP and the lipid moiety are both required for efficient biodistribution, fusion inhibition, and efficacy in vivo.pt_PT
dc.description.sponsorshipM.P. acknowledges grants R01AI121349 and R01AI119762 funded by the National Institutes of Health (NIH). T.N.F. acknowledges individual fellowships SFRH/BD/5283/2013 funded by Fundação para a Ciência e a Tecnologia (FCTMCTES). A.S.V. acknowledges funding under the Investigator Programme (IF/00803/2012) from FCT-MCTES. This work was supported by FCT-MCTES projects PTDC/QEQ-MED/4412/2014 and PTDC/BBB-BQB/3494/2014pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationBioconjugate Chem. 2018, 29, 3362−3376pt_PT
dc.identifier.doi10.1021/acs.bioconjchem.8b00527pt_PT
dc.identifier.issn1043-1802
dc.identifier.urihttp://hdl.handle.net/10451/37658
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherAmerican Chemical Societypt_PT
dc.relationSFRH/BD/5283/2013pt_PT
dc.relationIF/00803/2012pt_PT
dc.relationTowards the development of innovative highly effective dual action anti-HIV peptides
dc.relationBroad-spectrum antiviral peptides against respiratory viruses
dc.relation.publisherversionhttps://pubs.acs.org/journal/bcchespt_PT
dc.titleEffective in vivo targeting of influenza virus through a cell-penetrating/fusion inhibitor tandem peptide anchored to the plasma membranept_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleTowards the development of innovative highly effective dual action anti-HIV peptides
oaire.awardTitleBroad-spectrum antiviral peptides against respiratory viruses
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FQEQ-MED%2F4412%2F2014/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBBB-BQB%2F3494%2F2014/PT
oaire.citation.endPage3376pt_PT
oaire.citation.startPage3362pt_PT
oaire.citation.titleBioconjugate Chemistrypt_PT
oaire.citation.volume29pt_PT
oaire.fundingStream3599-PPCDT
oaire.fundingStream3599-PPCDT
person.familyNameFigueira
person.familyNameVeiga
person.familyNameSantos
person.familyNameCastanho
person.givenNameTiago
person.givenNameAna Salome
person.givenNameNuno
person.givenNameMiguel
person.identifier.ciencia-idCD13-5E3A-A3C5
person.identifier.orcid0000-0002-0813-0745
person.identifier.orcid0000-0002-9892-2243
person.identifier.orcid0000-0002-0580-0475
person.identifier.orcid0000-0001-7891-7562
person.identifier.ridN-7248-2013
person.identifier.scopus-author-id56745037100
person.identifier.scopus-author-id55940818300
person.identifier.scopus-author-id56605575600
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.rightsrestrictedAccesspt_PT
rcaap.typearticlept_PT
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