Ocellatin-PT antimicrobial peptides: high-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems
| Autor(a) principal: | |
|---|---|
| Data de Publicação: | 2016 |
| Outros Autores: | , , , , , , , , , , |
| Tipo de documento: | Artigo |
| Idioma: | eng |
| Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
| Texto Completo: | http://hdl.handle.net/1822/42737 |
Resumo: | 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 -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. |
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Ocellatin-PT antimicrobial peptides: high-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systemsAntimicrobial peptidesAtomic force microscopyScanning electron microscopyLeishmania infantumLipid membranesSurface plasmon resonanceAlthough 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 -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.This work was partially supported by grants from INCT Nanobiotecnologia and PVE Project (MCT/CNPq), the Consejo Nacional de Investigaciones Cientificas y Técnicas (CONICET), and the Agencia Nacional de Promocion Científica y Tecnologica (ANPCyT). M.M.M.is a researcher at CONICET. This work has also been supported through project UID/MULTI/04378/2013-POCI/01/0145/FEDER/007728 with financial support from FCT/MEC through national funds and co-financed by FEDER, under the Partnership Agreement PT2020. Scanning electron microscopy was carried out at Centro de Materiais da Universidade do Porto, CEMUP. Peter Eaton is supported by a Ciência sem Fronteiras grant via CNPq, and his lab work is supported by financial support from FCT/MEC through national funds and co-financed by FEDER, under the partnership agreement PT2020. Alexandra Pl acido and Ana Georgina Gomes-Alves are grateful to FCT for their grants SFRH/BD/97995/2013 and SFRH/BD/93766/2013, financed by POPH–QREN–Tipologia 4.1–Formação Avançada, subsidized by Fundo Social Europeu and Ministério da Ciência, Tecnologia e Ensino Superior. Nuno Vale thanks Programa Operacional Regional do Norte (ON.2) and Faculdade de Ciências da Universidade do Porto (FCUP) for co-funding refurbishment of the Porto Peptide Synthesis Facility (POPUP) through operation NORTE-07-0162-FEDER000111. NV thanks Fundação para a Ciência e Tecnologia (FCT, Portugal) and FEDER (European Union) for funding through project grant IF/00092/2014. Work in AMT laboratory was supported by Project “NORTE-07-0124-FEDER-000002-Host-Pathogen Interactions” cofunded by Programa Operacional Regional do Norte under QREN, through FEDER and FCT. None of the funding bodies were involved in study design, in the collection, analysis and interpretation of data; in the writing of the report; or in the decision to submit the article for publication.John Wiley and SonsUniversidade do MinhoOliveira, MayaraAlves, Ana G. GomesSousa, CarlaMarani, Mariela MirtaPlácido, AlexandraVale, NunoDelerue-Matos, CristinaGameiro, PaulaKückelhaus, Selma A. S.Tomas, Ana M.Leite, José Roberto S. A.Eaton, Peter20162016-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/42737engOliveira, Mayara; Alves, A.; Sousa, Carla; Mirta Marani, Mariela; Plácido, Alexandra; Vale, Nuno; Delerue-Matos, Cristina; Gameiro, Paula; Kückelhaus, Selma A. S.; Tomas, Ana M.; Leite, José Roberto S. A.; Eaton, Peter, Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems. Biopolymers, 105(12), 873-886, 20160006-35251097-028210.1002/bip.2292527463422info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-21T12:09:21Zoai:repositorium.sdum.uminho.pt:1822/42737Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:00:44.054752Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
| 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 Scanning electron microscopy Leishmania infantum Lipid membranes 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 |
| author |
Oliveira, Mayara |
| author_facet |
Oliveira, Mayara Alves, Ana G. Gomes Sousa, Carla Marani, Mariela Mirta Plácido, Alexandra Vale, Nuno Delerue-Matos, Cristina Gameiro, Paula Kückelhaus, Selma A. S. Tomas, Ana M. Leite, José Roberto S. A. Eaton, Peter |
| author_role |
author |
| author2 |
Alves, Ana G. Gomes Sousa, Carla Marani, Mariela Mirta Plácido, Alexandra Vale, Nuno Delerue-Matos, Cristina Gameiro, Paula Kückelhaus, Selma A. S. Tomas, Ana M. Leite, José Roberto S. A. Eaton, Peter |
| author2_role |
author author author author author author author author author author author |
| dc.contributor.none.fl_str_mv |
Universidade do Minho |
| dc.contributor.author.fl_str_mv |
Oliveira, Mayara Alves, Ana G. Gomes Sousa, Carla Marani, Mariela Mirta Plácido, Alexandra Vale, Nuno Delerue-Matos, Cristina Gameiro, Paula Kückelhaus, Selma A. S. Tomas, Ana M. Leite, José Roberto S. A. Eaton, Peter |
| dc.subject.por.fl_str_mv |
Antimicrobial peptides Atomic force microscopy Scanning electron microscopy Leishmania infantum Lipid membranes Surface plasmon resonance |
| topic |
Antimicrobial peptides Atomic force microscopy Scanning electron microscopy Leishmania infantum Lipid membranes Surface plasmon resonance |
| 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 -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 2016-01-01T00:00:00Z |
| dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
| dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
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article |
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publishedVersion |
| dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/1822/42737 |
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http://hdl.handle.net/1822/42737 |
| dc.language.iso.fl_str_mv |
eng |
| language |
eng |
| dc.relation.none.fl_str_mv |
Oliveira, Mayara; Alves, A.; Sousa, Carla; Mirta Marani, Mariela; Plácido, Alexandra; Vale, Nuno; Delerue-Matos, Cristina; Gameiro, Paula; Kückelhaus, Selma A. S.; Tomas, Ana M.; Leite, José Roberto S. A.; Eaton, Peter, Ocellatin-PT antimicrobial peptides: High-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems. Biopolymers, 105(12), 873-886, 2016 0006-3525 1097-0282 10.1002/bip.22925 27463422 |
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info:eu-repo/semantics/openAccess |
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openAccess |
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application/pdf |
| dc.publisher.none.fl_str_mv |
John Wiley and Sons |
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John Wiley and Sons |
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