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Escherichia coli cell surface perturbation and disruption induced by antimicrobial peptides BP100 and pepR

dc.contributor.authorAlves, Carla S.
dc.contributor.authorMelo, Manuel N.
dc.contributor.authorFranquelim, Henri G.
dc.contributor.authorFerre, Rafael
dc.contributor.authorPlanas, Marta
dc.contributor.authorFeliu, Lidia
dc.contributor.authorBardají, Eduard
dc.contributor.authorKowalczyk, Wioleta
dc.contributor.authorAndreu, David
dc.contributor.authorSantos, Nuno C.
dc.contributor.authorFernandes, Miguel X.
dc.contributor.authorCastanho, Miguel A.R.B.
dc.date.accessioned2023-02-08T12:04:54Z
dc.date.available2023-02-08T12:04:54Z
dc.date.issued2010
dc.description.abstractThe potential of antimicrobial peptides (AMPs) as an alter native to conventional therapies is well recognized. Insights into the biological and biophysical properties of AMPs are thus key to understanding their mode of action. In this study, the mech anisms adopted by two AMPs in disrupting the Gram-negative Escherichia coli bacterial envelope were explored. BP100 is a short cecropin A-melittin hybrid peptide known to inhibit the growth of phytopathogenic Gram-negative bacteria. pepR, on the other hand, is a novel AMP derived from the dengue virus capsid protein. Both BP100 and pepR were found to inhibit the growth of E. coli at micromolar concentrations. Zeta potential measurements of E. coli incubated with increasing peptide concentrations allowed for the establishment of a correlation between the minimal inhibitory concentration (MIC) of each AMP and membrane surface charge neutralization. While a neutralization-mediated killing mechanism adopted by either AMP is not necessarily implied, the hypothesis that surface neu tralization occurs close to MIC values was confirmed. Atomic force microscopy (AFM) was then employed to visualize the structural effect of the interaction of each AMP with the E. coli cell envelope. At their MICs, BP100 and pepR progressively destroyed the bacterial envelope, with extensive damage already occurring 2 h after peptide addition to the bacteria. A similar effect was observed for each AMP in the concentration-depen dent studies. At peptide concentrations below MIC values, only minor disruptions of the bacterial surface occurred.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationAlves, C. S., Melo, M. N., Franquelim, H. G., Ferre, R., Planas, M., Feliu, L., ... & Castanho, M. A. (2010). Escherichia coli cell surface perturbation and disruption induced by antimicrobial peptides BP100 and pepR. Journal of Biological Chemistry, 285(36), 27536-27544.pt_PT
dc.identifier.doi10.1074/jbc.M110.130955pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.13/5014
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevierpt_PT
dc.relationDINÂMICA CONFORMACIONAL DO PÉPTIDO TRANSLOCADOR DE CÉLULAS PEP-1 EM SISTEMAS MODELO DE MEMBRANAS: ESTUDOS DE SIMULAÇÃO COMPUTACIONAL E ESPECTROSCÓPICOS
dc.relationESTUDO DO MECANISMO DE ACÇÃO DE PÉPTIDOS MICROBICIDAS RIBOSSOMAIS DE INTERESSE CLÍNICO
dc.relationESTUDO DO MECANISMO DE ACÇÃO DE PÉPTIDOS INIBIDORES DE FUSÃO DO HIV DE INTERESSE CLÍNICO COMPROVADO
dc.relationThe role of lipid membranes in Dengue virus cell infection
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/pt_PT
dc.subjectAntimicrobial peptidespt_PT
dc.subjectAtomic force microscopypt_PT
dc.subjectBacteriapt_PT
dc.subjectDynamic light scatteringpt_PT
dc.subjectMembrane structurept_PT
dc.subject.pt_PT
dc.subjectFaculdade de Ciências Exatas e da Engenhariapt_PT
dc.titleEscherichia coli cell surface perturbation and disruption induced by antimicrobial peptides BP100 and pepRpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleDINÂMICA CONFORMACIONAL DO PÉPTIDO TRANSLOCADOR DE CÉLULAS PEP-1 EM SISTEMAS MODELO DE MEMBRANAS: ESTUDOS DE SIMULAÇÃO COMPUTACIONAL E ESPECTROSCÓPICOS
oaire.awardTitleESTUDO DO MECANISMO DE ACÇÃO DE PÉPTIDOS MICROBICIDAS RIBOSSOMAIS DE INTERESSE CLÍNICO
oaire.awardTitleESTUDO DO MECANISMO DE ACÇÃO DE PÉPTIDOS INIBIDORES DE FUSÃO DO HIV DE INTERESSE CLÍNICO COMPROVADO
oaire.awardTitleThe role of lipid membranes in Dengue virus cell infection
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBD%2F24547%2F2005/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/PIDDAC/SFRH%2FBD%2F24778%2F2005/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBD%2F39039%2F2007/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FQUI%2F69937%2F2006/PT
oaire.citation.endPage27544pt_PT
oaire.citation.issue36pt_PT
oaire.citation.startPage27536pt_PT
oaire.citation.titleJournal of Biological Chemistrypt_PT
oaire.citation.volume285pt_PT
oaire.fundingStreamPIDDAC
oaire.fundingStream3599-PPCDT
person.familyNameAlves
person.familyNameFernandes
person.givenNameCarla Sophia
person.givenNameMiguel Xavier
person.identifier.ciencia-idED1D-3C7A-467C
person.identifier.orcid0000-0002-8891-5234
person.identifier.orcid0000-0002-1840-616X
person.identifier.ridA-4373-2013
person.identifier.scopus-author-id11438813200
person.identifier.scopus-author-id35466972500
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
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