28-mer fragment derived from enterocin CRL35 displays an unexpected bactericidal effect on listeria cells

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dc.contributor.authorMasias, Emilse
dc.contributor.authorSanches, Paulo R.S. [UNESP]
dc.contributor.authorDupuy, Fernando G.
dc.contributor.authorAcuña, Leonardo
dc.contributor.authorBellomio, Augusto
dc.contributor.authorCilli, Eduardo [UNESP]
dc.contributor.authorSaavedra, Lucila
dc.contributor.authorMinahk, Carlos
dc.contributor.institutionQuímica y Farmacia
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionCentro de Referencia Para Lactobacilos
dc.date.accessioned2019-01-09T12:47:15Z
dc.date.available2019-01-09T12:47:15Z
dc.date.issued2015-01-01
dc.description.abstractTwo shorter peptides derived from enterocin CRL35, a 43-mer bacteriocin, were synthesized i. e. the N-terminal fragment spanning from residues 1 to 15, and a 28-mer fragment that represents the Cterminal of enterocin CRL35, the residues 16 to 43. The separate peptides showed no activity when combined. On one hand, the 28-mer peptide displayed an unpredicted antimicrobial activity. On the other, 15mer peptide had no consistent anti-Listeria effect. The dissociation constants calculated from experimental data indicated that all peptides could bind at similar extent to the sensitive cells. However, transmembrane electrical potential was not dissipated to the same level by the different peptides; whereas the full-length and the C-terminal 28-mer fragment induced almost full dissipation, 15-mer fragment produced only a slow and incomplete effect. Furthermore, a different interaction of each peptide with membranes was demonstrated based on studies carried out with liposomes, which led us to conclude that activity was related to structure rather than to net positive charges. These results open up the possibility of designing new peptides based on the 28-mer fragment with enhanced activity, which would represent a promising approach for combating Listeria and other pathogens.en
dc.description.affiliationInstituto Superior de Investigaciones Biológicas (INSIBIO) CONICET-UNT Facultad de Bioquímica Química y Farmacia, UNT. Chacabuco 461
dc.description.affiliationDepartamento de Bioquímica e Tecnologia Química Instituto de Química UNESP-Univ Estadual Paulista
dc.description.affiliationCentro de Referencia Para Lactobacilos, Chacabuco 145
dc.description.affiliationUnespUniversidade Estadual Paulista Júlio de Mesquita Filho, Instituto de Química de Araraquara, Departamento de Bioquímica e Tecnologia Química
dc.description.sponsorshipConsejo Nacional de Investigaciones Cientificas y Tecnicas
dc.description.sponsorshipSecretaria de Ciencia y Tecnica de la Universidad Nacional de Tucuman
dc.description.sponsorshipAgencia Nacional de Promocion Cientifica y Tecnologica
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipCONICET
dc.description.sponsorshipIdConsejo Nacional de Investigaciones Cientificas y Tecnicas: PIP 0779
dc.description.sponsorshipIdConsejo Nacional de Investigaciones Cientificas y Tecnicas: PIP 0183
dc.description.sponsorshipIdSecretaria de Ciencia y Tecnica de la Universidad Nacional de Tucuman: 26/D228
dc.description.sponsorshipIdSecretaria de Ciencia y Tecnica de la Universidad Nacional de Tucuman: PIUNT D548/1
dc.description.sponsorshipIdAgencia Nacional de Promocion Cientifica y Tecnologica: PICT 1295
dc.description.sponsorshipIdAgencia Nacional de Promocion Cientifica y Tecnologica: PICT 2998
dc.format.extent482-488
dc.identifierhttp://dx.doi.org/10.2174/0929866522666150506094300
dc.identifier.citationProtein And Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 22, n. 6, p. 482-488, 2015.
dc.identifier.doi10.2174/0929866522666150506094300
dc.identifier.issn1875-5305
dc.identifier.issn0929-8665
dc.identifier.orcid0000-0002-4767-0904
dc.identifier.urihttp://hdl.handle.net/11449/190737
dc.language.isoeng
dc.publisherBentham Science Publ Ltd
dc.relation.ispartofProtein and Peptide Letters
dc.relation.ispartofjcr1.039
dc.relation.ispartofsjr0,429
dc.relation.isreplacedbydouble182746*
dc.rights.accessRightsAcesso restrito
dc.subjectBacteriocins
dc.subjectEnterocin CRL35
dc.subjectListeria
dc.subjectSynthetic peptides
dc.title28-mer fragment derived from enterocin CRL35 displays an unexpected bactericidal effect on listeria cellsen
dc.typeArtigo
dcterms.rightsHolderBentham Science Publ Ltd
unesp.author.orcid0000-0002-4767-0904[6]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Química, Araraquarapt

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