Self-assembly and intracellular delivery of DNA by a truncated fragment derived from the Trojan peptide Penetratin

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dc.audience.educationlevel
dc.contributor.authorSilva, Emerson Rodrigo
dc.contributor.authorLatteshttp://lattes.cnpq.br/7800589206457326pt_BR
dc.coverage.spatialReino Unidopt_BR
dc.date.accessioned2021-01-14T11:10:43Z
dc.date.available2021-01-14T11:10:43Z
dc.date.issued17-04-20
dc.description.provenanceSubmitted by Emerson Rodrigo da Silva (er.silva@unifesp.br) on 2020-05-14T14:29:37Z No. of bitstreams: 2 article_KIW-R1clean.docx: 4654899 bytes, checksum: 35913e3d199e92cd8b16842bb5d2847c (MD5) SUPPORTING INFORMATION KIW-R1.docx: 2980233 bytes, checksum: c5aa96e00b15c245934f0fc1b4b93e74 (MD5)en
dc.description.provenanceApproved for entry into archive by Mariusa Loução (mariusa.loucao@unifesp.br) on 2021-01-14T11:10:43Z (GMT) No. of bitstreams: 2 article_KIW-R1clean.docx: 4654899 bytes, checksum: 35913e3d199e92cd8b16842bb5d2847c (MD5) SUPPORTING INFORMATION KIW-R1.docx: 2980233 bytes, checksum: c5aa96e00b15c245934f0fc1b4b93e74 (MD5)en
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dc.description.resumoPenetratin is a short Trojan peptide that attracts great interest in biomedical research for its capacity to translocate biological membranes. Herein, we study in detail both self-assembly and intracellular delivery of DNA by the heptamer KIWFQNR, a truncated peptide derived from Penetratin. This shortened sequence possesses a unique design with bolaamphiphilic characteristics that preserves the longest noncationic amino acid portion found in Penetratin. These features convey amphipathicity to assist self-assembly and make it a suitable model for exploring the role of hydrophobic residues for peptide interaction and cell uptake. We show that the fragment forms peptiplexes (i.e., peptide-DNA complexes), and aggregates into long nanofibers with clear beta-sheet signature. The supramolecular structure of nanofibers likely comprises DNA cores surrounded by a peptide shell for which the double helix behaves as a template and induces fibrillization. A nucleation and growth mechanism proceeding through liquid-liquid phase separation of coacervates is proposed for describing the self-assembly of peptiplexes. We also demonstrate that peptiplexes deliver double-stranded 200bp DNA into HeLa cells, indicating its potential for preparing non-viral vectors for oligonucleotides through noncovalent strategies. Since the main structural features of native Penetratin are conserved in this simpler fragment, our findings also highlight the role of uncharged amino acids for structuration, and thus for the ability of Penetratin to cross cell membranes.pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.identifierhttps://pubs.rsc.org/en/content/articlelanding/2020/SM/D0SM00347F#!divAbstractpt_BR
dc.identifier.doi10.1039/D0SM00347Fpt_BR
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/59025
dc.languageengpt_BR
dc.publisherRoyal Society of Chemistrypt_BR
dc.relation.ispartofSoft Matterpt_BR
dc.rightsAcesso abertopt_BR
dc.subjectPeptídeopt_BR
dc.subjectNanoestrutura
dc.subjectTerapia gênica
dc.subjectBiofísica estrutural
dc.subjectMicroscopia de força atômica
dc.subjectEspalhamento a baixo ângulo
dc.titleSelf-assembly and intracellular delivery of DNA by a truncated fragment derived from the Trojan peptide Penetratinpt_BR
dc.title.alternativeSelf-assembly and intracellular delivery of DNA by a truncated fragment derived from the Trojan peptide penetratinpt_BR
dc.typeArtigopt_BR
unifesp.campusEscola Paulista de Medicina (EPM)pt_BR
unifesp.departamentoBiofísicapt_BR
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