Electrostatic immobilization of antimicrobial peptides on polyethylenimine and their antibacterial effect against Staphylococcus epidermidis

dc.contributor.authorHernandez-Montelongo, J.
dc.contributor.authorCorrales Urena, Y. R.
dc.contributor.authorMachado, D.
dc.contributor.authorLancelloti, M.
dc.contributor.authorPinheiro, M. P.
dc.contributor.authorRischka, K.
dc.contributor.authorLisboa-Filho, P. N. [UNESP]
dc.contributor.authorCotta, M. A.
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionUniv Catolica Temuco
dc.contributor.institutionCtr Natl Alta Tecnol
dc.contributor.institutionFraunhofer Inst Mfg Technol & Adv Mat
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2018-11-26T17:49:06Z
dc.date.available2018-11-26T17:49:06Z
dc.date.issued2018-04-01
dc.description.abstractStaphylococcus epidermidis is a gram-positive bacterium, and one of the most prevalent causes of nosocomial infections due to its strong ability to form biofilms on catheters and surgical implants. Here we explore the antimicrobial properties of Tet-124 peptides, which are part of the innate defense against different multicellular organisms in nature. Two different Tet-124 peptides were immobilized on a polyethylenimine (PEI) film to determine their impact on the antimicrobial properties: KLWWMIRRW (Tet-124), which contains only natural amino acids, and KLWWMIRRWG-(F-Br)-G (F-Br- 4-Bromophenylalanine), a modified Tet-124 sequence with the addition of an unnatural amino acid. The immobilization was obtained as a result of the electrostatic interaction between PEI amino groups and the C-terminal carboxylic groups of tryptophan and glycine amino acids of Tet-124 and Tet-124-Br peptides, respectively. The process was monitored and studied by water contact angle, Atomic Force Microscopy (AFM), X-ray Photoelectron Spectroscopy (XPS) and Quartz Crystal Microbalance with Dissipation (QCM-D) measurements. The antibacterial effect of our samples against S. epidermis was evaluated by the spread plate counting method, and cytotoxicity was tested using fibroblast cultures. Our results indicate the feasibility to immobilize electrostatically both Tet-124 peptides for biomedical applications. (C) 2018 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv Estadual Campinas, Inst Fis Gleb Wataghin, Dept Fis Aplicada, BR-13083859 Campinas, SP, Brazil
dc.description.affiliationUniv Catolica Temuco, Fac Ingn, Dept Ciencias Matemat & Fis, Temuco 4813302, Chile
dc.description.affiliationUniv Catolica Temuco, Fac Ingn, Nucleo Invest Bioprod & Mat Avanzados BioMa, Temuco 4781312, Chile
dc.description.affiliationCtr Natl Alta Tecnol, Lab Nacl Nanotecnol, San Jose 11741200, Costa Rica
dc.description.affiliationUniv Estadual Campinas, Fac Ciencias Farmaceut, BR-13083871 Campinas, SP, Brazil
dc.description.affiliationFraunhofer Inst Mfg Technol & Adv Mat, D-28359 Bremen, Germany
dc.description.affiliationUniv Estadual Paulista, Fac Ciencias, Dept Fis, BR-17033360 Bauru, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Fac Ciencias, Dept Fis, BR-17033360 Bauru, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipIdFAPESP: 2013/14888-3
dc.description.sponsorshipIdFAPESP: 2015/16611-4
dc.format.extent370-378
dc.identifierhttp://dx.doi.org/10.1016/j.colsurfb.2018.02.002
dc.identifier.citationColloids And Surfaces B-biointerfaces. Amsterdam: Elsevier Science Bv, v. 164, p. 370-378, 2018.
dc.identifier.doi10.1016/j.colsurfb.2018.02.002
dc.identifier.fileWOS000429762100043.pdf
dc.identifier.issn0927-7765
dc.identifier.lattes1353862414532005
dc.identifier.orcid0000-0002-7734-4069
dc.identifier.urihttp://hdl.handle.net/11449/164098
dc.identifier.wosWOS:000429762100043
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofColloids And Surfaces B-biointerfaces
dc.relation.ispartofsjr1,071
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.subjectElectrostatic immobilization
dc.subjectAntimicrobial peptides
dc.subjectStaphylococcus epidermidis
dc.titleElectrostatic immobilization of antimicrobial peptides on polyethylenimine and their antibacterial effect against Staphylococcus epidermidisen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes1353862414532005[7]
unesp.author.orcid0000-0002-7734-4069[7]
unesp.departmentFísica - FCpt

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