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

Autores
Oliveira, Mayara; Gomes Alves, Ana G.; Sousa, Carla; Marani, Mariela Mirta; Plácido, Alexandra; Vale, Nuno; Delerue Matos, Cristina; Gameiro, Paula; Kückelhaus, Selma A. S.; Tomas, Ana M.; Leite, José Roberto de Souza Almeida; Eaton, Peter
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Although 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 α‐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.
Fil: Oliveira, Mayara. Universidade do Brasília; Brasil. Universidad de Porto; Portugal
Fil: Gomes Alves, Ana G.. Universidad de Porto; Portugal. Universidade Do Minho; Portugal
Fil: Sousa, Carla. Universidad de Porto; Portugal
Fil: Marani, Mariela Mirta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Instituto Patagónico para el Estudio de los Ecosistemas Continentales; Argentina
Fil: Plácido, Alexandra. Instituto Politécnico do Porto; Portugal
Fil: Vale, Nuno. Universidad de Porto; Portugal
Fil: Delerue Matos, Cristina. Instituto Politécnico do Porto; Portugal
Fil: Gameiro, Paula. Universidad de Porto; Portugal
Fil: Kückelhaus, Selma A. S.. Universidade do Brasília; Brasil
Fil: Tomas, Ana M.. Universidad de Porto; Portugal
Fil: Leite, José Roberto de Souza Almeida. Universidad de Porto; Portugal. Universidade do Brasília; Brasil. Universidade Federal do Piauí; Brasil
Fil: Eaton, Peter. Universidad de Porto; Portugal. Universidade Federal do Piauí; Brasil
Materia
Antimicrobial Peptides
Atomic Force Microscopy
Leishmania Infantum
Lipid Membranes
Scanning Electron Microscopy
Surface Plasmon Resonance
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/39471
Acceder
id CONICETDig_081172d4dd8b834a732c8328252fea80
oai_identifier_str oai:ri.conicet.gov.ar:11336/39471
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systemsOliveira, MayaraGomes Alves, Ana G.Sousa, CarlaMarani, Mariela MirtaPlácido, AlexandraVale, NunoDelerue Matos, CristinaGameiro, PaulaKückelhaus, Selma A. S.Tomas, Ana M.Leite, José Roberto de Souza AlmeidaEaton, PeterAntimicrobial PeptidesAtomic Force MicroscopyLeishmania InfantumLipid MembranesScanning Electron MicroscopySurface Plasmon Resonancehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Although 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 α‐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.Fil: Oliveira, Mayara. Universidade do Brasília; Brasil. Universidad de Porto; PortugalFil: Gomes Alves, Ana G.. Universidad de Porto; Portugal. Universidade Do Minho; PortugalFil: Sousa, Carla. Universidad de Porto; PortugalFil: Marani, Mariela Mirta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Instituto Patagónico para el Estudio de los Ecosistemas Continentales; ArgentinaFil: Plácido, Alexandra. Instituto Politécnico do Porto; PortugalFil: Vale, Nuno. Universidad de Porto; PortugalFil: Delerue Matos, Cristina. Instituto Politécnico do Porto; PortugalFil: Gameiro, Paula. Universidad de Porto; PortugalFil: Kückelhaus, Selma A. S.. Universidade do Brasília; BrasilFil: Tomas, Ana M.. Universidad de Porto; PortugalFil: Leite, José Roberto de Souza Almeida. Universidad de Porto; Portugal. Universidade do Brasília; Brasil. Universidade Federal do Piauí; BrasilFil: Eaton, Peter. Universidad de Porto; Portugal. Universidade Federal do Piauí; BrasilJohn Wiley & Sons Inc2016-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/39471Oliveira, Mayara; Gomes Alves, Ana G.; Sousa, Carla; Marani, Mariela Mirta; Plácido, Alexandra; et al.; Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems; John Wiley & Sons Inc; Biopolymers; 105; 12; 12-2016; 873-8860006-3525CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1002/bip.22925info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/bip.22925info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:03:26Zoai:ri.conicet.gov.ar:11336/39471instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:03:26.849CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems
title Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems
spellingShingle Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems
Oliveira, Mayara
Antimicrobial Peptides
Atomic Force Microscopy
Leishmania Infantum
Lipid Membranes
Scanning Electron Microscopy
Surface Plasmon Resonance
title_short Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems
title_full Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems
title_fullStr Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems
title_full_unstemmed Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems
title_sort Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems
dc.creator.none.fl_str_mv Oliveira, Mayara
Gomes Alves, Ana G.
Sousa, Carla
Marani, Mariela Mirta
Plácido, Alexandra
Vale, Nuno
Delerue Matos, Cristina
Gameiro, Paula
Kückelhaus, Selma A. S.
Tomas, Ana M.
Leite, José Roberto de Souza Almeida
Eaton, Peter
author Oliveira, Mayara
author_facet Oliveira, Mayara
Gomes Alves, Ana G.
Sousa, Carla
Marani, Mariela Mirta
Plácido, Alexandra
Vale, Nuno
Delerue Matos, Cristina
Gameiro, Paula
Kückelhaus, Selma A. S.
Tomas, Ana M.
Leite, José Roberto de Souza Almeida
Eaton, Peter
author_role author
author2 Gomes Alves, Ana G.
Sousa, Carla
Marani, Mariela Mirta
Plácido, Alexandra
Vale, Nuno
Delerue Matos, Cristina
Gameiro, Paula
Kückelhaus, Selma A. S.
Tomas, Ana M.
Leite, José Roberto de Souza Almeida
Eaton, Peter
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Antimicrobial Peptides
Atomic Force Microscopy
Leishmania Infantum
Lipid Membranes
Scanning Electron Microscopy
Surface Plasmon Resonance
topic Antimicrobial Peptides
Atomic Force Microscopy
Leishmania Infantum
Lipid Membranes
Scanning Electron Microscopy
Surface Plasmon Resonance
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Although 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 α‐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.
Fil: Oliveira, Mayara. Universidade do Brasília; Brasil. Universidad de Porto; Portugal
Fil: Gomes Alves, Ana G.. Universidad de Porto; Portugal. Universidade Do Minho; Portugal
Fil: Sousa, Carla. Universidad de Porto; Portugal
Fil: Marani, Mariela Mirta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Instituto Patagónico para el Estudio de los Ecosistemas Continentales; Argentina
Fil: Plácido, Alexandra. Instituto Politécnico do Porto; Portugal
Fil: Vale, Nuno. Universidad de Porto; Portugal
Fil: Delerue Matos, Cristina. Instituto Politécnico do Porto; Portugal
Fil: Gameiro, Paula. Universidad de Porto; Portugal
Fil: Kückelhaus, Selma A. S.. Universidade do Brasília; Brasil
Fil: Tomas, Ana M.. Universidad de Porto; Portugal
Fil: Leite, José Roberto de Souza Almeida. Universidad de Porto; Portugal. Universidade do Brasília; Brasil. Universidade Federal do Piauí; Brasil
Fil: Eaton, Peter. Universidad de Porto; Portugal. Universidade Federal do Piauí; Brasil
description Although 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 α‐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.
publishDate 2016
dc.date.none.fl_str_mv 2016-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/39471
Oliveira, Mayara; Gomes Alves, Ana G.; Sousa, Carla; Marani, Mariela Mirta; Plácido, Alexandra; et al.; Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems; John Wiley & Sons Inc; Biopolymers; 105; 12; 12-2016; 873-886
0006-3525
CONICET Digital
CONICET
url http://hdl.handle.net/11336/39471
identifier_str_mv Oliveira, Mayara; Gomes Alves, Ana G.; Sousa, Carla; Marani, Mariela Mirta; Plácido, Alexandra; et al.; Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems; John Wiley & Sons Inc; Biopolymers; 105; 12; 12-2016; 873-886
0006-3525
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1002/bip.22925
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/bip.22925
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv John Wiley & Sons Inc
publisher.none.fl_str_mv John Wiley & Sons Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846781267114196992
score 12.982451

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