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Structural studies of a lipid-binding peptide from tunicate hemocytes with anti-biofilm activity

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dc.contributor.authorSilva, Osmar N.
dc.contributor.authorAlves, Eliane S. F.
dc.contributor.authorFuente-Núñez, César de la
dc.contributor.authorRibeiro, Suzana M.
dc.contributor.authorMandal, Santi M.
dc.contributor.authorGaspar, Diana
dc.contributor.authorVeiga, Ana S.
dc.contributor.authorCastanho, Miguel A. R. B.
dc.contributor.authorAndrade, Cesar A. S.
dc.contributor.authorNascimento, Jessica M.
dc.contributor.authorFensterseifer, Isabel C. M.
dc.contributor.authorPorto, William F.
dc.contributor.authorCorrea, Jose R.
dc.contributor.authorHancock, Robert. E. W.
dc.contributor.authorKorpole, Suresh Korpole
dc.contributor.authorOliveira, Aline L.
dc.contributor.authorLiao, Luciano M.
dc.contributor.authorFranco, Octavio L.
dc.date.accessioned2018-04-16T13:35:59Z
dc.date.available2018-04-16T13:35:59Z
dc.date.issued2016
dc.descriptionThis work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/pt_PT
dc.description.abstractClavanins is a class of peptides (23aa) histidine-rich, free of post-translational modifications. Clavanins have been studied largely for their ability to disrupt bacterial membranes. In the present study, the interaction of clavanin A with membranes was assessed by dynamic light scattering, zeta potential and permeabilization assays. We observed through those assays that clavanin A lysis bacterial cells at concentrations corresponding to its MIC. Further, the structure and function of clavanin A was investigated. To better understand how clavanin interacted with bacteria, its NMR structure was elucidated. The solution state NMR structure of clavanin A in the presence of TFE-d3 indicated an α-helical conformation. Secondary structures, based on circular dichroism measurements in anionic sodium dodecyl sulfate (SDS) and TFE (2,2,2-trifluorethanol), in silico lipid-peptide docking and molecular simulations with lipids DPPC and DOPC revealed that clavanin A can adopt a variety of folds, possibly influencing its different functions. Microcalorimetry assays revealed that clavanin A was capable of discriminating between different lipids. Finally, clavanin A was found to eradicate bacterial biofilms representing a previously unrecognized function.pt_PT
dc.description.sponsorshipWe would like to thank CNPq, CAPES (Ciências sem Fronteiras), FAPDF and FUNDECT. D.G. acknowledges Fundação para a Ciência e a Tecnologia - Ministério da Educação e Ciência (FCT-MEC, Portugal) for fellowship SFRH/BPD/73500/2010 and A.S.V. for funding within the FCT Investigator Programme (IF/00803/2012).pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.doi10.1038/srep27128pt_PT
dc.identifier.issn0144-8463
dc.identifier.urihttp://hdl.handle.net/10451/32817
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherPortland Presspt_PT
dc.relationIF/00803/2012pt_PT
dc.relationSTUDYING AND DEVELOPING ANTIMICROBIAL PEPTIDE HYDROGELS USED IN TISSUE REGENERATION
dc.relation.publisherversionhttp://www.bioscirep.org/pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.titleStructural studies of a lipid-binding peptide from tunicate hemocytes with anti-biofilm activitypt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleSTUDYING AND DEVELOPING ANTIMICROBIAL PEPTIDE HYDROGELS USED IN TISSUE REGENERATION
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBPD%2F73500%2F2010/PT
oaire.citation.startPage27128pt_PT
oaire.citation.titleBioscience Reportspt_PT
oaire.citation.volume6pt_PT
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isProjectOfPublication8aef3bd6-260c-4cad-afd0-15952a73f08e
relation.isProjectOfPublication.latestForDiscovery8aef3bd6-260c-4cad-afd0-15952a73f08e

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