Logo do repositório
 
Publicação

A polyalanine peptide derived from polar fish with anti-infectious activities

dc.contributor.authorCardoso, Marlon H.
dc.contributor.authorRibeiro, Suzana M.
dc.contributor.authorNolasco, Diego O.
dc.contributor.authorFuente-Núñez, César de la
dc.contributor.authorFelício, Mário Romão
dc.contributor.authorAbreu, Sónia Gonçalves
dc.contributor.authorMatos, Carolina O.
dc.contributor.authorLiao, Luciano M.
dc.contributor.authorSantos, Nuno C.
dc.contributor.authorHancock, Robert E. W.
dc.contributor.authorFranco, Octávio L.
dc.contributor.authorMigliolo, Ludovico
dc.date.accessioned2019-04-02T11:27:31Z
dc.date.available2019-04-02T11:27:31Z
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/4pt_PT
dc.description.abstractDue to the growing concern about antibiotic-resistant microbial infections, increasing support has been given to new drug discovery programs. A promising alternative to counter bacterial infections includes the antimicrobial peptides (AMPs), which have emerged as model molecules for rational design strategies. Here we focused on the study of Pa-MAP 1.9, a rationally designed AMP derived from the polar fish Pleuronectes americanus. Pa-MAP 1.9 was active against Gram-negative planktonic bacteria and biofilms, without being cytotoxic to mammalian cells. By using AFM, leakage assays, CD spectroscopy and in silico tools, we found that Pa-MAP 1.9 may be acting both on intracellular targets and on the bacterial surface, also being more efficient at interacting with anionic LUVs mimicking Gram-negative bacterial surface, where this peptide adopts α-helical conformations, than cholesterolenriched LUVs mimicking mammalian cells. Thus, as bacteria present varied physiological features that favor antibiotic-resistance, Pa-MAP 1.9 could be a promising candidate in the development of tools against infections caused by pathogenic bacteria.pt_PT
dc.description.sponsorshipResearch reported in this publication was supported by the National Institute of Allergy and Infectious Diseases of the National Institutes of Health under Award Number R21AI098701, and by a grant from the Canadian Institutes. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. R.E.W.H. holds a Canada Research Chair in Health and Genomics. C.D.L.F.-N. received a scholarship from the Fundación “la Caixa” and Fundación Canadá (Spain), and currently holds a postdoctoral scholarship from Fundación Ramón Areces (Spain). This work was also supported by Fundaçao para a Ciencia e a Tecnologia–Ministério da Educaçao e Ciencia (FCT-MEC, Portugal), including the fellowship SPRH/BD/100517/2014 to M.R.F., and by Marie Skłodowska-Curie Research and Innovation Staff Exchange (MSCA-RISE, European Union) project INPACT (call H2020-MSCA-RISE-2014, grant agreement 644167). M.H.C., L.M. and O.L.F. acknowledge funding from CNPq, CAPES, FUNDECT and FAPDF.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationScientific Reports | 6:21385pt_PT
dc.identifier.doi10.1038/srep21385pt_PT
dc.identifier.issn2045-2322
dc.identifier.urihttp://hdl.handle.net/10451/37805
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherNature Researchpt_PT
dc.relationSPRH/BD/100517/2014pt_PT
dc.relationH2020-MSCA-RISE-2014pt_PT
dc.relation644167pt_PT
dc.relation.publisherversionhttps://www.nature.com/srep/pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.titleA polyalanine peptide derived from polar fish with anti-infectious activitiespt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.startPage21385pt_PT
oaire.citation.titleScientific Reportspt_PT
oaire.citation.volume6pt_PT
person.familyNameRomão Felício
person.familyNameAbreu
person.familyNameSantos
person.givenNameMário
person.givenNameSónia
person.givenNameNuno
person.identifier384205
person.identifier.ciencia-idF811-74AE-412A
person.identifier.ciencia-idCD13-5E3A-A3C5
person.identifier.orcid0000-0002-9398-2140
person.identifier.orcid0000-0003-2903-4282
person.identifier.orcid0000-0002-0580-0475
person.identifier.ridJ-8517-2014
person.identifier.ridH-9482-2017
person.identifier.ridN-7248-2013
person.identifier.scopus-author-id57144367400
person.identifier.scopus-author-id35602210000
person.identifier.scopus-author-id55940818300
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication8d7bbafe-ae5e-418e-8224-6af22991a3e7
relation.isAuthorOfPublicationc077a1e4-3d11-47c7-b5d4-29a5a4190a35
relation.isAuthorOfPublication4656d912-5a2d-4c80-8921-2bcba3aa441a
relation.isAuthorOfPublication.latestForDiscoveryc077a1e4-3d11-47c7-b5d4-29a5a4190a35

Ficheiros

Principais
A mostrar 1 - 1 de 1
A carregar...
Miniatura
Nome:
Polyalanine_peptide.pdf
Tamanho:
2.07 MB
Formato:
Adobe Portable Document Format