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A designed cyclic analogue of gomesin has potent activity against Staphylococcus aureus biofilms

2022Artigo científico Acesso aberto
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dc.contributor.authorDias, Susana
dc.contributor.authorPinto, Sandra
dc.contributor.authorSilva-Herdade, Ana S.
dc.contributor.authorCheneval, Olivier
dc.contributor.authorCraik, David J
dc.contributor.authorCoutinho, Ana
dc.contributor.authorCastanho, Miguel A. R. B.
dc.contributor.authorHenriques, Sónia T.
dc.contributor.authorVeiga, Ana Salomé
dc.date.accessioned2022-09-30T14:32:39Z
dc.date.available2022-09-30T14:32:39Z
dc.date.issued2022
dc.description© The Author(s) 2022. Published by Oxford University Press on behalf of British Society for Antimicrobial Chemotherapy. This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https:// creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.compt_PT
dc.description.abstractBackground: Infections caused by bacterial biofilms are very difficult to treat. The use of currently approved antibiotics even at high dosages often fails, making the treatment of these infections very challenging. Novel antimicrobial agents that use distinct mechanisms of action are urgently needed. Objectives: To explore the use of [G1K,K8R]cGm, a designed cyclic analogue of the antimicrobial peptide gomesin, as an alternative approach to treat biofilm infections. Methods: We studied the activity of [G1K,K8R]cGm against biofilms of Staphylococcus aureus, a pathogen associated with several biofilm-related infections. A combination of atomic force and real-time confocal laser scanning microscopies was used to study the mechanism of action of the peptide. Results: The peptide demonstrated potent activity against 24 h-preformed biofilms through a concentration-dependent ability to kill biofilm-embedded cells. Mechanistic studies showed that [G1K,K8R]cGm causes morphological changes on bacterial cells and permeabilizes their membranes across the biofilm with a half-time of 65 min. We also tested an analogue of [G1K,K8R]cGm without disulphide bonds, and a linear unfolded analogue, and found both to be inactive. Conclusions: The results suggest that the 3D structure of [G1K,K8R]cGm and its stabilization by disulphide bonds are essential for its antibacterial and antibiofilm activities. Moreover, our findings support the potential application of this stable cyclic antimicrobial peptide to fight bacterial biofilms.pt_PT
dc.description.sponsorshipThis project received funding from the European Union’s Horizon 2020 research and innovation programme under grant agreement No. 828774. This work was supported by project grants funded by Fundação para a Ciência e a Tecnologia (FCT-MCTES, Portugal; UIDB/04565/2020 and PPBI-POCI-01-0145-FEDER-022122). S.A.D. acknowledges FCT for the fellowship PD/BD/114425/2016. S.T.H. is an Australian Research Council (ARC) Future Fellow (FT150100398) and is supported by the ARC Centre of Excellence for Innovations in Peptide & Protein Science (CE200100012).pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationJ Antimicrob Chemother. 2022 Sep 29;dkac309pt_PT
dc.identifier.doi10.1093/jac/dkac309pt_PT
dc.identifier.eissn1460-2091
dc.identifier.issn0305-7453
dc.identifier.urihttp://hdl.handle.net/10451/54640
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherOxford University Presspt_PT
dc.relation828774pt_PT
dc.relationInstitute for Bioengineering and Biosciences
dc.relationTowards the development of antimicrobial peptides active against bacterial biofilms
dc.relation.publisherversionhttps://academic.oup.com/jacpt_PT
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/pt_PT
dc.titleA designed cyclic analogue of gomesin has potent activity against Staphylococcus aureus biofilmspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleInstitute for Bioengineering and Biosciences
oaire.awardTitleTowards the development of antimicrobial peptides active against bacterial biofilms
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04565%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//PD%2FBD%2F114425%2F2016/PT
oaire.citation.titleJournal of Antimicrobial Chemotherapypt_PT
oaire.fundingStream6817 - DCRRNI ID
person.familyNameDias
person.familyNamePinto
person.familyNameSilva-Herdade
person.familyNameCoutinho
person.familyNameCastanho
person.familyNameVeiga
person.givenNameSusana
person.givenNameSandra
person.givenNameAna S.
person.givenNameAna
person.givenNameMiguel
person.givenNameAna Salome
person.identifier749915
person.identifierC-3755-2014
person.identifier.ciencia-idF61D-0A28-659A
person.identifier.ciencia-idDF1B-B557-85AF
person.identifier.ciencia-id6517-B340-F362
person.identifier.ciencia-idCC1F-2174-161A
person.identifier.orcid0000-0001-8910-5404
person.identifier.orcid0000-0002-3205-9459
person.identifier.orcid0000-0002-3023-1315
person.identifier.orcid0000-0003-1653-0703
person.identifier.orcid0000-0001-7891-7562
person.identifier.orcid0000-0002-9892-2243
person.identifier.ridH-8446-2016
person.identifier.ridB-2735-2019
person.identifier.scopus-author-id25637336300
person.identifier.scopus-author-id56605575600
person.identifier.scopus-author-id56745037100
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
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
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