The importance of cyclic structure for Labaditin on its antimicrobial activity against Staphylococcus aureus

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dc.contributor.authorBarbosa, Simone C.
dc.contributor.authorNobre, Thatyane M.
dc.contributor.authorVolpati, Diogo
dc.contributor.authorCiancaglini, Pietro
dc.contributor.authorCilli, Eduardo M. [UNESP]
dc.contributor.authorLorenzon, Esteban N.
dc.contributor.authorOliveira, Osvaldo N.
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionMid Sweden Univ
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Federal de Goiás (UFG)
dc.date.accessioned2018-11-26T17:55:56Z
dc.date.available2018-11-26T17:55:56Z
dc.date.issued2016-12-01
dc.description.abstractAntimicrobial resistance has reached alarming levels in many countries, thus leading to a search for new classes of antibiotics, such as antimicrobial peptides whose activity is exerted by interacting specifically with the microorganism membrane. In this study, we investigate the molecular-level mechanism of action for Labaditin (Lo), a 10-amino acid residue cyclic peptide from Jatropha multifida with known bactericidal activity against Streptococcus mutans. We show that Lo is also effective against Staphylococcus aureus (S. aureus) but this does not apply to its linear analogue (L-1). Using polarization-modulated infrared reflection absorption spectroscopy (PM-IRRAS), we observed with that the secondary structure of Lo was preserved upon interacting with Langmuir monolayers from a phospholipid mixture mimicking S. aureus membrane, in contrast to L-1. This structure preservation for the rigid, cyclic Lo is key for the self-assembly of peptide nanotubes that induce pore formation in large unilamellar vesicles (LUVs), according to permeability assays and dynamic light scattering measurements. In summary, the comparison between Labaditin (Lo) and its linear analogue L-1 allowed us to infer that the bactericidal activity of Lo is more related to its interaction with the membrane. It does not require specific metabolic targets, which makes cyclic peptides promising for antibiotics without bacteria resistance. (C) 2016 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv Sao Paulo, Inst Fis Sao Carlos, Sao Carlos, SP, Brazil
dc.description.affiliationMid Sweden Univ, Dept Nat Sci, SE-85170 Sundsvall, Sweden
dc.description.affiliationUniv Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Quim, Ribeirao Preto, SP, Brazil
dc.description.affiliationUniv Estadual Paulista, Inst Quim, Araraquara, SP, Brazil
dc.description.affiliationUniv Fed Goias, Inst Ciencias Biol, Dept Bioquim & Biol Mol, Goiania, Go, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Inst Quim, Araraquara, SP, Brazil
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipnBioNet network (Brazil)
dc.description.sponsorshipIdFAPESP: 2014/03748-9
dc.format.extent453-459
dc.identifierhttp://dx.doi.org/10.1016/j.colsurfb.2016.09.017
dc.identifier.citationColloids And Surfaces B-biointerfaces. Amsterdam: Elsevier Science Bv, v. 148, p. 453-459, 2016.
dc.identifier.doi10.1016/j.colsurfb.2016.09.017
dc.identifier.fileWOS000388248500051.pdf
dc.identifier.issn0927-7765
dc.identifier.urihttp://hdl.handle.net/11449/164747
dc.identifier.wosWOS:000388248500051
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofColloids And Surfaces B-biointerfaces
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.subjectAntimicrobial peptide
dc.subjectCyclic peptides
dc.subjectPeptide nanotubes
dc.subjectLabaditin
dc.subjectLangmuir monolayers
dc.subjectPM-IRRAS
dc.subjectLarge unilamellar vesicles
dc.subjectStaphylococcus aureus
dc.titleThe importance of cyclic structure for Labaditin on its antimicrobial activity against Staphylococcus aureusen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.orcid0000-0002-2785-1345[4]

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