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EcDBS1R4, an antimicrobial peptide effective against Escherichia coli with in vitro fusogenic ability

2020-11-30Artigo científico Acesso aberto
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dc.contributor.authorMakowski, Marcin
dc.contributor.authorFelício, Mário Romão
dc.contributor.authorFensterseifer, Isabel C M
dc.contributor.authorFranco, Octávio L
dc.contributor.authorSantos, Nuno C.
dc.contributor.authorGonçalves, Sónia
dc.date.accessioned2021-04-06T12:20:57Z
dc.date.available2021-04-06T12:20:57Z
dc.date.issued2020-11-30
dc.description©2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open accessarticle distributed under the terms and conditions of the Creative Commons Attribution(CC BY) license (http://creativecommons.org/licenses/by/4.0/)pt_PT
dc.description.abstractDiscovering antibiotic molecules able to hold the growing spread of antimicrobial resistance is one of the most urgent endeavors that public health must tackle. The case of Gram-negative bacterial pathogens is of special concern, as they are intrinsically resistant to many antibiotics, due to an outer membrane that constitutes an effective permeability barrier. Antimicrobial peptides (AMPs) have been pointed out as potential alternatives to conventional antibiotics, as their main mechanism of action is membrane disruption, arguably less prone to elicit resistance in pathogens. Here, we investigate the in vitro activity and selectivity of EcDBS1R4, a bioinspired AMP. To this purpose, we have used bacterial cells and model membrane systems mimicking both the inner and the outer membranes of Escherichia coli, and a variety of optical spectroscopic methodologies. EcDBS1R4 is effective against the Gram-negative E. coli, ineffective against the Gram-positive Staphylococcus aureus and noncytotoxic for human cells. EcDBS1R4 does not form stable pores in E. coli, as the peptide does not dissipate its membrane potential, suggesting an unusual mechanism of action. Interestingly, EcDBS1R4 promotes a hemi-fusion of vesicles mimicking the inner membrane of E. coli. This fusogenic ability of EcDBS1R4 requires the presence of phospholipids with a negative curvature and a negative charge. This finding suggests that EcDBS1R4 promotes a large lipid spatial reorganization able to reshape membrane curvature, with interesting biological implications herein discussed.pt_PT
dc.description.sponsorshipThis research was funded by Fundação para a Ciência e a Tecnologia—Ministério da Ciência, Tecnologia e Ensino Superior (FCT-MCTES, Portugal), Marie Skłodowska-Curie Research and Innovation Staff Exchange (MSCA-RISE, European Union) project INPACT (call H2020-MSCA-RISE-2014, grant agreement 644167), Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq, Brazil), Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES, Brazil), Fundação de Amparo a Pesquisa do Distrito Federal (FAPDF, Brazil) and Fundação de Apoio ao Desenvolvimento do Ensino, Ciência e Tecnologia do Estado de Mato Grosso do Sul (FUNDECT, Brazil). M.M. and M.R.F. also acknowledge FCT-MCTES fellowships SPRH/BD/128290/2017 and SPRH/BD/100517/2014, respectively.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationInt J Mol Sci. 2020 Nov 30;21(23):9104pt_PT
dc.identifier.doi10.3390/ijms21239104pt_PT
dc.identifier.eissn1422-0067
dc.identifier.issn1661-6596
dc.identifier.urihttp://hdl.handle.net/10451/47250
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherMDPIpt_PT
dc.relationSPRH/BD/128290/2017pt_PT
dc.relationInnovative peptides against cancer and pathogenic bacteria, with advances in science, biopharmaceutical drug development, product market targeting, training , and communication.
dc.relation.publisherversionhttps://www.mdpi.com/journal/ijmspt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectAntimicrobial peptidept_PT
dc.subjectEcDBS1R4pt_PT
dc.subjectCardiolipinpt_PT
dc.subjectGram-negative bacteriapt_PT
dc.subjectEscherichia colipt_PT
dc.subjectHemifusionpt_PT
dc.subjectHyperpolarizationpt_PT
dc.titleEcDBS1R4, an antimicrobial peptide effective against Escherichia coli with in vitro fusogenic abilitypt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardNumber644167
oaire.awardTitleInnovative peptides against cancer and pathogenic bacteria, with advances in science, biopharmaceutical drug development, product market targeting, training , and communication.
oaire.awardURIinfo:eu-repo/grantAgreement/EC/H2020/644167/EU
oaire.citation.issue23pt_PT
oaire.citation.titleInternational Journal of Molecular Sciencespt_PT
oaire.citation.volume21pt_PT
oaire.fundingStreamH2020
person.familyNameMakowski
person.familyNameRomão Felício
person.familyNameSantos
person.familyNameAbreu
person.givenNameMarcin
person.givenNameMário
person.givenNameNuno
person.givenNameSónia
person.identifier384205
person.identifier.ciencia-idE81F-976B-0C55
person.identifier.ciencia-idCD13-5E3A-A3C5
person.identifier.ciencia-idF811-74AE-412A
person.identifier.orcid0000-0001-6929-6143
person.identifier.orcid0000-0002-9398-2140
person.identifier.orcid0000-0002-0580-0475
person.identifier.orcid0000-0003-2903-4282
person.identifier.ridJ-8517-2014
person.identifier.ridN-7248-2013
person.identifier.ridH-9482-2017
person.identifier.scopus-author-id57144367400
person.identifier.scopus-author-id55940818300
person.identifier.scopus-author-id35602210000
project.funder.identifierhttp://doi.org/10.13039/501100008530
project.funder.nameEuropean Commission
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
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relation.isAuthorOfPublication8d7bbafe-ae5e-418e-8224-6af22991a3e7
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relation.isAuthorOfPublication.latestForDiscovery4656d912-5a2d-4c80-8921-2bcba3aa441a
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