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dc.contributor.authorBrand, Guilherme Dotto-
dc.contributor.authorRamada, Marcelo Henrique Soller-
dc.contributor.authorManickchand, Júlia R.-
dc.contributor.authorCorrea, Rafael-
dc.contributor.authorRibeiro, Dalila J. S.-
dc.contributor.authorSantos, Michele A.-
dc.contributor.authorVasconcelos, Andreanne Gomes-
dc.contributor.authorAbrão, Fernando Y.-
dc.contributor.authorPrates, Maura V.-
dc.contributor.authorMurad, André M.-
dc.contributor.authorCardozo Filho, José de Lima-
dc.contributor.authorLeite, José Roberto de Souza de Almeida-
dc.contributor.authorMagalhães, Kelly G.-
dc.contributor.authorOliveira, Aline Lima de-
dc.contributor.authorBloch Júnior, Carlos-
dc.date.accessioned2019-11-11T14:41:10Z-
dc.date.available2019-11-11T14:41:10Z-
dc.date.issued2019-
dc.identifier.citationBRAND, GUILHERME D. et al. Intragenic antimicrobial peptides (IAPs) from human proteins with potent antimicrobial and anti-inflammatory activity. PLoS ONE, v. 14, n. 8, e0220656, 2019. DOI: https://doi.org/10.1371/journal.pone.0220656. Disponível em: https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0220656. Acesso em: 11 nov. 2019.pt_BR
dc.identifier.urihttps://repositorio.unb.br/handle/10482/35803-
dc.language.isoInglêspt_BR
dc.publisherPlos Onept_BR
dc.rightsAcesso Abertopt_BR
dc.titleIntragenic antimicrobial peptides (IAPs) from human proteins with potent antimicrobial and anti-inflammatory activitypt_BR
dc.typeArtigopt_BR
dc.subject.keywordPeptídeos bioativospt_BR
dc.subject.keywordAgentes antiinflamatóriospt_BR
dc.subject.keywordAgentes antiinfecciosospt_BR
dc.rights.license© 2019 Brand et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.pt_BR
dc.description.abstract1Following the treads of our previous works on the unveiling of bioactive peptides encrypted in plant proteins from diverse species, the present manuscript reports the occurrence of four proof-of-concept intragenic antimicrobial peptides in human proteins, named Hs IAPs. These IAPs were prospected using the software Kamal, synthesized by solid phase chemistry, and had their interactions with model phospholipid vesicles investigated by differential scanning calorimetry and circular dichroism. Their antimicrobial activity against bacteria, yeasts and filamentous fungi was determined, along with their cytotoxicity towards erythrocytes. Our data demonstrates that Hs IAPs are capable to bind model membranes while attaining α-helical structure, and to inhibit the growth of microorganisms at concentrations as low as 1μM. Hs02, a novel sixteen residue long internal peptide (KWAVRIIRKFIKGFISNH2) derived from the unconventional myosin 1h protein, was further investigated in its capacity to inhibit lipopolysaccharide-induced release of TNF-α in murine macrophages. Hs02 presented potent anti-inflammatory activity, inhibiting the release of TNF-α in LPSprimed cells at the lowest assayed concentration, 0.1 μM. A three-dimensional solution structure of Hs02 bound to DPC micelles was determined by Nuclear Magnetic Resonance. Our work exemplifies how the human genome can be mined for molecules with biotechnological potential in human health and demonstrates that IAPs are actual alternatives to antimicrobial peptides as pharmaceutical agents or in their many other putative applications.pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-1615-0009pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-6928-078Xpt_BR
dc.description.unidadeInstituto de Química (IQ)pt_BR
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