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Antibiofilm activity on Candida albicans and mechanism of action on biomembrane models of the antimicrobial peptide Ctn(15–34)

2020Journal article Open access
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dc.contributor.authorAguiar, Francisca Lidiane Linhares de
dc.contributor.authorSantos, Nuno C.
dc.contributor.authorde Paula Cavalcante, Carolina Sidrim
dc.contributor.authorAndreu, David
dc.contributor.authorBaptista, Gandhi Radis
dc.contributor.authorGonçalves, Sónia
dc.date.accessioned2021-04-07T13:00:04Z
dc.date.available2021-04-07T13:00:04Z
dc.date.issued2020
dc.description© 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article 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.abstractCtn[15-34], the C-terminal fragment of crotalicidin, an antimicrobial peptide from the South American rattlesnake Crotalus durissus terrificus venom, displays remarkable anti-infective and anti-proliferative activities. Herein, its activity on Candida albicans biofilms and its interaction with the cytoplasmic membrane of the fungal cell and with a biomembrane model in vitro was investigated. A standard C. albicans strain and a fluconazole-resistant clinical isolate were exposed to the peptide at its minimum inhibitory concentration (MIC) (10 µM) and up to 100 × MIC to inhibit biofilm formation and its eradication. A viability test using XTT and fluorescent dyes, confocal laser scanning microscopy, and atomic force microscopy (AFM) were used to observe the antibiofilm effect. To evaluate the importance of membrane composition on Ctn[15-34] activity, C. albicans protoplasts were also tested. Fluorescence assays using di-8-ANEPPS, dynamic light scattering, and zeta potential measurements using liposomes, protoplasts, and C. albicans cells indicated a direct mechanism of action that was dependent on membrane interaction and disruption. Overall, Ctn[15-34] showed to be an effective antifungal peptide, displaying antibiofilm activity and, importantly, interacting with and disrupting fungal plasma membrane.pt_PT
dc.description.sponsorshipThis research was funded by the Coordination for the Improvement of Higher Education Personnel (CAPES), Finance Code 001, from the Ministry of Education and Culture (MEC), Federal Government of Brazil (F.L.L.d.A.), and by Fundação para a Ciência e a Tecnologia—Ministério da Ciência, Tecnologia e Ensino Superior (FCT-MCTES, Portugal). Partial research funding was from the National Council of Research and Development, (CNPq), the Ministry of Science, Technology and Innovation (MCTI), grant numbers 307733/2016-5 and 431077/2016-9 (G.R.B.).pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationInt J Mol Sci. 2020 Nov 6;21(21):8339pt_PT
dc.identifier.doi10.3390/ijms21218339pt_PT
dc.identifier.eissn1422-0067
dc.identifier.issn1661-6596
dc.identifier.urihttp://hdl.handle.net/10451/47276
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherMDPIpt_PT
dc.relation307733/2016-5pt_PT
dc.relation431077/2016-9pt_PT
dc.relation.publisherversionhttps://www.mdpi.com/journal/ijmspt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectCandida albicanspt_PT
dc.subjectAntimicrobial peptidept_PT
dc.subjectBiofilmpt_PT
dc.subjectBiomembranept_PT
dc.subjectCrotalicidinpt_PT
dc.subjectMembrane-active peptidept_PT
dc.subjectVenom-derived peptidept_PT
dc.subjectYeast protoplastpt_PT
dc.titleAntibiofilm activity on Candida albicans and mechanism of action on biomembrane models of the antimicrobial peptide Ctn(15–34)pt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.issue21pt_PT
oaire.citation.titleInternational Journal of Molecular Sciencespt_PT
oaire.citation.volume21pt_PT
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT

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