Publication
Escherichia coli cell surface perturbation and disruption induced by antimicrobial peptides BP100 and pepR
dc.contributor.author | Alves, Carla S. | |
dc.contributor.author | Melo, Manuel N. | |
dc.contributor.author | Franquelim, Henri G. | |
dc.contributor.author | Ferre, Rafael | |
dc.contributor.author | Planas, Marta | |
dc.contributor.author | Feliu, Lidia | |
dc.contributor.author | Bardají, Eduard | |
dc.contributor.author | Kowalczyk, Wioleta | |
dc.contributor.author | Andreu, David | |
dc.contributor.author | Santos, Nuno C. | |
dc.contributor.author | Fernandes, Miguel X. | |
dc.contributor.author | Castanho, Miguel A.R.B. | |
dc.date.accessioned | 2023-02-08T12:04:54Z | |
dc.date.available | 2023-02-08T12:04:54Z | |
dc.date.issued | 2010 | |
dc.description.abstract | The 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.version | info:eu-repo/semantics/publishedVersion | pt_PT |
dc.identifier.citation | Alves, 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.doi | 10.1074/jbc.M110.130955 | pt_PT |
dc.identifier.uri | http://hdl.handle.net/10400.13/5014 | |
dc.language.iso | eng | pt_PT |
dc.peerreviewed | yes | pt_PT |
dc.publisher | Elsevier | pt_PT |
dc.relation | DINÂMICA CONFORMACIONAL DO PÉPTIDO TRANSLOCADOR DE CÉLULAS PEP-1 EM SISTEMAS MODELO DE MEMBRANAS: ESTUDOS DE SIMULAÇÃO COMPUTACIONAL E ESPECTROSCÓPICOS | |
dc.relation | ESTUDO DO MECANISMO DE ACÇÃO DE PÉPTIDOS MICROBICIDAS RIBOSSOMAIS DE INTERESSE CLÍNICO | |
dc.relation | ESTUDO DO MECANISMO DE ACÇÃO DE PÉPTIDOS INIBIDORES DE FUSÃO DO HIV DE INTERESSE CLÍNICO COMPROVADO | |
dc.relation | The role of lipid membranes in Dengue virus cell infection | |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | pt_PT |
dc.subject | Antimicrobial peptides | pt_PT |
dc.subject | Atomic force microscopy | pt_PT |
dc.subject | Bacteria | pt_PT |
dc.subject | Dynamic light scattering | pt_PT |
dc.subject | Membrane structure | pt_PT |
dc.subject | . | pt_PT |
dc.subject | Faculdade de Ciências Exatas e da Engenharia | pt_PT |
dc.title | Escherichia coli cell surface perturbation and disruption induced by antimicrobial peptides BP100 and pepR | pt_PT |
dc.type | journal article | |
dspace.entity.type | Publication | |
oaire.awardTitle | DINÂMICA CONFORMACIONAL DO PÉPTIDO TRANSLOCADOR DE CÉLULAS PEP-1 EM SISTEMAS MODELO DE MEMBRANAS: ESTUDOS DE SIMULAÇÃO COMPUTACIONAL E ESPECTROSCÓPICOS | |
oaire.awardTitle | ESTUDO DO MECANISMO DE ACÇÃO DE PÉPTIDOS MICROBICIDAS RIBOSSOMAIS DE INTERESSE CLÍNICO | |
oaire.awardTitle | ESTUDO DO MECANISMO DE ACÇÃO DE PÉPTIDOS INIBIDORES DE FUSÃO DO HIV DE INTERESSE CLÍNICO COMPROVADO | |
oaire.awardTitle | The role of lipid membranes in Dengue virus cell infection | |
oaire.awardURI | info:eu-repo/grantAgreement/FCT//SFRH%2FBD%2F24547%2F2005/PT | |
oaire.awardURI | info:eu-repo/grantAgreement/FCT/PIDDAC/SFRH%2FBD%2F24778%2F2005/PT | |
oaire.awardURI | info:eu-repo/grantAgreement/FCT//SFRH%2FBD%2F39039%2F2007/PT | |
oaire.awardURI | info:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FQUI%2F69937%2F2006/PT | |
oaire.citation.endPage | 27544 | pt_PT |
oaire.citation.issue | 36 | pt_PT |
oaire.citation.startPage | 27536 | pt_PT |
oaire.citation.title | Journal of Biological Chemistry | pt_PT |
oaire.citation.volume | 285 | pt_PT |
oaire.fundingStream | PIDDAC | |
oaire.fundingStream | 3599-PPCDT | |
person.familyName | Alves | |
person.familyName | Fernandes | |
person.givenName | Carla Sophia | |
person.givenName | Miguel Xavier | |
person.identifier.ciencia-id | ED1D-3C7A-467C | |
person.identifier.orcid | 0000-0002-8891-5234 | |
person.identifier.orcid | 0000-0002-1840-616X | |
person.identifier.rid | A-4373-2013 | |
person.identifier.scopus-author-id | 11438813200 | |
person.identifier.scopus-author-id | 35466972500 | |
project.funder.identifier | http://doi.org/10.13039/501100001871 | |
project.funder.identifier | http://doi.org/10.13039/501100001871 | |
project.funder.identifier | http://doi.org/10.13039/501100001871 | |
project.funder.identifier | http://doi.org/10.13039/501100001871 | |
project.funder.name | Fundação para a Ciência e a Tecnologia | |
project.funder.name | Fundação para a Ciência e a Tecnologia | |
project.funder.name | Fundação para a Ciência e a Tecnologia | |
project.funder.name | Fundação para a Ciência e a Tecnologia | |
rcaap.rights | openAccess | pt_PT |
rcaap.type | article | pt_PT |
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relation.isAuthorOfPublication.latestForDiscovery | a94320e0-abf7-4fcb-a607-966133a78f3e | |
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