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dc.contributor.authorMariano, G. H.-
dc.contributor.authorSá, Luís Guilherme Gomes de-
dc.contributor.authorSilva, E. M. Carmo da-
dc.contributor.authorSantos, M. A.-
dc.contributor.authorCardozo Filho, José de Lima-
dc.contributor.authorLira, B. O. V.-
dc.contributor.authorBarbosa, Eder Alves-
dc.contributor.authorAraujo, A. R.-
dc.contributor.authorLeite, José Roberto de Souza de Almeida-
dc.contributor.authorRamada, Marcelo Henrique Soller-
dc.contributor.authorBloch Júnior, Carlos-
dc.contributor.authorOliveira, Aline Lima de-
dc.contributor.authorChaker, Juliano Alexandre-
dc.contributor.authorBrand, Guilherme Dotto-
dc.date.accessioned2023-10-18T11:38:32Z-
dc.date.available2023-10-18T11:38:32Z-
dc.date.issued2020-10-01-
dc.identifier.citationMARIANO, G. H. et al. Characterization of novel human intragenic antimicrobial peptides, incorporation and release studies from ureasil-polyether hybrid matrix. Materials Science and Engineering: C, [S.l.], v. 119, 111581, fev. 2021. DOI: https://doi.org/10.1016/j.msec.2020.111581.pt_BR
dc.identifier.urihttp://repositorio2.unb.br/jspui/handle/10482/46697-
dc.language.isoengpt_BR
dc.publisherElsevier B.V.pt_BR
dc.rightsAcesso Restritopt_BR
dc.titleCharacterization of novel human intragenic antimicrobial peptides, incorporation and release studies from ureasil-polyether hybrid matrixpt_BR
dc.typeArtigopt_BR
dc.subject.keywordPeptídeos antimicrobianospt_BR
dc.subject.keywordMineração de dados (Computação)pt_BR
dc.subject.keywordFilmes poliméricospt_BR
dc.subject.keywordPolímerospt_BR
dc.identifier.doihttps://doi.org/10.1016/j.msec.2020.111581pt_BR
dc.relation.publisherversionhttps://www.sciencedirect.com/science/article/pii/S0928493120334998?via%3Dihubpt_BR
dc.description.abstract1Intragenic antimicrobial peptides (IAPs) are internal sequences of proteins with physicochemical similarities to Antimicrobial Peptides (AMPs) that, once identified and synthesized as individual entities, present antimicrobial activity. Many mature proteins encoded by the genomes of virtually any organism may be regarded as inner reservoirs of IAPs, conferring them ample biotechnological potential. However, IAPs may also share shortcomings with AMPs, such as low half-life in biological media and non-specific adsorption in eukaryotic cells. The present manuscript reports a translational approach that encompasses the uncovering of two novel IAPs from human proteins as well as the first results concerning the incorporation and sustained release of one of these peptides from ureasil-polyether hybrid polymeric films. For such, the software Kamal was used to scan putative IAPs in the human proteome, and two peptides, named Hs05 and Hs06, were identified, synthesized, and tested as antimicrobials. Biophysical assays were conducted using model phospholipid vesicles and 1H NMR solution structures in phospholipid micelles were obtained for the IAP Hs05. This peptide was incorporated in a polymeric matrix composed of the ureasil/PPO-PEO-PPO triblock copolymer, and the resulting films were evaluated by atomic force microscopy and imaging mass spectrometry. The release rate of Hs05 from the polymeric matrix was assessed and the antimicrobial activity of Hs05-loaded hybrid polymeric films was evaluated against the bacterium Escherichia coli. This study represents the first steps towards the development of polymeric films enriched with IAPs obtained from the human proteome as sustained release devices for topical application.pt_BR
dc.contributor.affiliationUniversidade de Brasília, Instituto de Química, Laboratório de Síntese e Análise de Biomoléculaspt_BR
dc.contributor.affiliationUniversidade de Brasília, Instituto de Química, Laboratório de Síntese e Análise de Biomoléculaspt_BR
dc.contributor.affiliationUniversidade de Brasília, Instituto de Química, Laboratório de Ressonância Magnética Nuclearpt_BR
dc.contributor.affiliationUniversidade de Brasília, Instituto de Química, Laboratório de Ressonância Magnética Nuclearpt_BR
dc.contributor.affiliationEmbrapa Recursos Genéticos e Biotecnologia, Laboratório de Espectrometria de Massapt_BR
dc.contributor.affiliationUniversidade Católica de Brasília, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologiapt_BR
dc.contributor.affiliationUniversidade de Brasília, Instituto de Química, Laboratório de Síntese e Análise de Biomoléculaspt_BR
dc.contributor.affiliationUniversidade Federal do Delta do Parnaíba, Núcleo de Pesquisa em Biodiversidade e Biotecnologiapt_BR
dc.contributor.affiliationUniversidade de Brasília, Faculdade de Medicina, Núcleo de Pesquisa em Morfologia e Imunologia Aplicadapt_BR
dc.contributor.affiliationUniversidade Católica de Brasília, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologiapt_BR
dc.contributor.affiliationUniversidade Católica de Brasília, Programa de Pós-Graduação em Gerontologiapt_BR
dc.contributor.affiliationEmbrapa Recursos Genéticos e Biotecnologia, Laboratório de Espectrometria de Massapt_BR
dc.contributor.affiliationUniversidade de Brasília, Instituto de Química, Laboratório de Ressonância Magnética Nuclearpt_BR
dc.contributor.affiliationUniversidade de Brasília, Faculdade da Ceilândiapt_BR
dc.contributor.affiliationUniversidade de Brasília, Instituto de Química, Laboratório de Síntese e Análise de Biomoléculaspt_BR
dc.description.unidadeInstituto de Química (IQ)pt_BR
dc.description.unidadeFaculdade de Medicina (FMD)pt_BR
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