Repository logo
 
Publication

Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems

2016Journal article Restricted access
Simple item page
dc.contributor.authorOliveira, Mayara
dc.contributor.authorGomes-Alves, Ana Georgina
dc.contributor.authorSousa, Carla
dc.contributor.authorMarani, Mariela Mirta
dc.contributor.authorPlácido, Alexandra
dc.contributor.authorVale, Nuno
dc.contributor.authorDelerue-Matos, Cristina
dc.contributor.authorGameiro, Paula
dc.contributor.authorKuckelhaus, Selma A. S.
dc.contributor.authorTomás, Ana M.
dc.contributor.authorLeite, José Roberto S. A.
dc.contributor.authorEaton, Peter
dc.date.accessioned2017-01-11T12:29:16Z
dc.date.embargo2116
dc.date.issued2016
dc.description.abstractAlthough the mechanism of action of antimicrobial peptides (AMPs) is not clear, they can interact electrostatically with the cell membranes of microorganisms. New ocellatin-PT peptides were recently isolated from the skin secretion of Leptodactylus pustulatus. The secondary structure of these AMPs and their effect on Leishmania infantum cells, and on different lipid surface models was characterized in this work. The results showed that all ocellatin-PT peptides have an a-helix structure and five of them (PT3, PT4, PT6 to PT8) have leishmanicidal activity; PT1 and PT2 affected the cellular morphology of the parasites and showed greater affinity for leishmania and bacteria-mimicking lipid membranes than for those of mammals. The results show selectivity of ocellatin-PTs to the membranes of microorganisms and the applicability of biophysical methods to clarify the interaction of AMPs with cell membranes.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.doi10.1002/bip.22925pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.22/9212
dc.language.isoengpt_PT
dc.publisherWileypt_PT
dc.relation.ispartofseriesBiopolymers;Volume 105, Issue 12
dc.relation.publisherversionhttp://onlinelibrary.wiley.com/doi/10.1002/bip.22925/abstractpt_PT
dc.subjectAntimicrobial peptidespt_PT
dc.subjectAtomic force microscopypt_PT
dc.subjectScanning electron microscopypt_PT
dc.subjectLeishmania infantumpt_PT
dc.subjectLipid membranespt_PT
dc.subjectSurface plasmon resonancept_PT
dc.titleOcellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systemspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.titleBiopolymerspt_PT
person.familyNameDelerue-Matos
person.givenNameCristina
person.identifier.ciencia-id9A1A-43FB-5C27
person.identifier.orcid0000-0002-3924-776X
person.identifier.ridD-4990-2013
person.identifier.scopus-author-id6603741848
rcaap.rightsclosedAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication09f6a7bd-2f15-42b0-adc5-04bd22210519
relation.isAuthorOfPublication.latestForDiscovery09f6a7bd-2f15-42b0-adc5-04bd22210519

Files

Original bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
ART_MatosCristina_GRAQ_2016.pdf
Size:
1.59 MB
Format:
Adobe Portable Document Format
Download
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
1.71 KB
Format:
Item-specific license agreed upon to submission
Description:
Download

Collections

ISEP – GRAQ – Artigos