Development of a novel anti-biofilm peptide derived from profilin ofSpodoptera frugiperda
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1080/08927014.2020.1776857 http://hdl.handle.net/11449/197047 |
Resumo: | Candidayeast infections are the fourth leading cause of death worldwide. Peptides with antimicrobial activity are a promising alternative treatment for such infections. Here, the antifungal activity of a new antimicrobial peptide-PEP-IA18-was evaluated againstCandidaspecies. PEP-IA18 was designed from the primary sequence of profilin, a protein fromSpodoptera frugiperda,and displayed potent activity againstCandida albicansandCandida tropicalis, showing a minimum inhibitory concentration (MIC) of 2.5 mu M. Furthermore, the mechanism of action of PEP-IA18 involved interaction with the cell membrane (ergosterol complexation). Treatment at MIC and/or 10 x MIC significantly reduced biofilm formation and viability. PEP-IA18 showed low toxicity toward human fibroblasts and only revealed hemolytic activity at high concentrations. Thus, PEP-IA18 exhibited antifungal and anti-biofilm properties with potential applicability in the treatment of infections caused byCandidaspecies. |
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Repositório Institucional da UNESP |
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spelling |
Development of a novel anti-biofilm peptide derived from profilin ofSpodoptera frugiperdaAntifungalbiofilmCandida spppeptideCandidayeast infections are the fourth leading cause of death worldwide. Peptides with antimicrobial activity are a promising alternative treatment for such infections. Here, the antifungal activity of a new antimicrobial peptide-PEP-IA18-was evaluated againstCandidaspecies. PEP-IA18 was designed from the primary sequence of profilin, a protein fromSpodoptera frugiperda,and displayed potent activity againstCandida albicansandCandida tropicalis, showing a minimum inhibitory concentration (MIC) of 2.5 mu M. Furthermore, the mechanism of action of PEP-IA18 involved interaction with the cell membrane (ergosterol complexation). Treatment at MIC and/or 10 x MIC significantly reduced biofilm formation and viability. PEP-IA18 showed low toxicity toward human fibroblasts and only revealed hemolytic activity at high concentrations. Thus, PEP-IA18 exhibited antifungal and anti-biofilm properties with potential applicability in the treatment of infections caused byCandidaspecies.Fundacao de Apoio ao Desenvolvimento do Ensino, Ciencia e Tecnologia do Estado de Mato Grosso do SulUniv Fed Mato Grosso, Fac Pharmaceut Sci Food & Nutr, Prot Purificat Lab & Biol Funct, Campo Grande, MS, BrazilFed Univ Grande Dourados, Ctr Biotechnol & Bioprospecting Studies Appl Meta, Dourados, MS, BrazilSao Paulo State Univ, Inst Chem, Dept Biochem, Araraquara, SP, BrazilUniv Catolica Dom Bosco, Grad Program Biotechnol, S Inova Biotech, Campo Grande, MS, BrazilUniv Catolica Brasilia, Ctr Prote & Biochem Anal, Grad Program Genom Sci & Biotechnol, Brasilia, DF, BrazilUniv Brasilia, Fac Med, Grad Program Mol Pathol, Brasilia, DF, BrazilSao Paulo State Univ, Inst Chem, Dept Biochem, Araraquara, SP, BrazilFundacao de Apoio ao Desenvolvimento do Ensino, Ciencia e Tecnologia do Estado de Mato Grosso do Sul: 08/2015Taylor & Francis LtdUniversidade Federal de Mato Grosso do Sul (UFMS)Fed Univ Grande DouradosUniversidade Estadual Paulista (Unesp)Univ Catolica Dom BoscoUniv Catolica BrasiliaUniversidade de Brasília (UnB)Borges da Silva, Amanda CarolinaOrlandi Sardi, Janaina de CassiaLourenco de Oliveira, Daniella GoreteRamalho de Oliveira, Caio FernandoSantos, Helder Freitas dosSantos, Edson Lucas dosCrusca Jr, Edson [UNESP]Cardoso, Marlon HenriqueFranco, Octavio LuizRodrigues Macedo, Maria Ligia2020-12-10T20:04:30Z2020-12-10T20:04:30Z2020-07-02info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article11http://dx.doi.org/10.1080/08927014.2020.1776857Biofouling. Abingdon: Taylor & Francis Ltd, 11 p., 2020.0892-7014http://hdl.handle.net/11449/19704710.1080/08927014.2020.1776857WOS:000546318700001Web of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBiofoulinginfo:eu-repo/semantics/openAccess2021-10-23T10:31:40Zoai:repositorio.unesp.br:11449/197047Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462021-10-23T10:31:40Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Development of a novel anti-biofilm peptide derived from profilin ofSpodoptera frugiperda |
title |
Development of a novel anti-biofilm peptide derived from profilin ofSpodoptera frugiperda |
spellingShingle |
Development of a novel anti-biofilm peptide derived from profilin ofSpodoptera frugiperda Borges da Silva, Amanda Carolina Antifungal biofilm Candida spp peptide |
title_short |
Development of a novel anti-biofilm peptide derived from profilin ofSpodoptera frugiperda |
title_full |
Development of a novel anti-biofilm peptide derived from profilin ofSpodoptera frugiperda |
title_fullStr |
Development of a novel anti-biofilm peptide derived from profilin ofSpodoptera frugiperda |
title_full_unstemmed |
Development of a novel anti-biofilm peptide derived from profilin ofSpodoptera frugiperda |
title_sort |
Development of a novel anti-biofilm peptide derived from profilin ofSpodoptera frugiperda |
author |
Borges da Silva, Amanda Carolina |
author_facet |
Borges da Silva, Amanda Carolina Orlandi Sardi, Janaina de Cassia Lourenco de Oliveira, Daniella Gorete Ramalho de Oliveira, Caio Fernando Santos, Helder Freitas dos Santos, Edson Lucas dos Crusca Jr, Edson [UNESP] Cardoso, Marlon Henrique Franco, Octavio Luiz Rodrigues Macedo, Maria Ligia |
author_role |
author |
author2 |
Orlandi Sardi, Janaina de Cassia Lourenco de Oliveira, Daniella Gorete Ramalho de Oliveira, Caio Fernando Santos, Helder Freitas dos Santos, Edson Lucas dos Crusca Jr, Edson [UNESP] Cardoso, Marlon Henrique Franco, Octavio Luiz Rodrigues Macedo, Maria Ligia |
author2_role |
author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Federal de Mato Grosso do Sul (UFMS) Fed Univ Grande Dourados Universidade Estadual Paulista (Unesp) Univ Catolica Dom Bosco Univ Catolica Brasilia Universidade de Brasília (UnB) |
dc.contributor.author.fl_str_mv |
Borges da Silva, Amanda Carolina Orlandi Sardi, Janaina de Cassia Lourenco de Oliveira, Daniella Gorete Ramalho de Oliveira, Caio Fernando Santos, Helder Freitas dos Santos, Edson Lucas dos Crusca Jr, Edson [UNESP] Cardoso, Marlon Henrique Franco, Octavio Luiz Rodrigues Macedo, Maria Ligia |
dc.subject.por.fl_str_mv |
Antifungal biofilm Candida spp peptide |
topic |
Antifungal biofilm Candida spp peptide |
description |
Candidayeast infections are the fourth leading cause of death worldwide. Peptides with antimicrobial activity are a promising alternative treatment for such infections. Here, the antifungal activity of a new antimicrobial peptide-PEP-IA18-was evaluated againstCandidaspecies. PEP-IA18 was designed from the primary sequence of profilin, a protein fromSpodoptera frugiperda,and displayed potent activity againstCandida albicansandCandida tropicalis, showing a minimum inhibitory concentration (MIC) of 2.5 mu M. Furthermore, the mechanism of action of PEP-IA18 involved interaction with the cell membrane (ergosterol complexation). Treatment at MIC and/or 10 x MIC significantly reduced biofilm formation and viability. PEP-IA18 showed low toxicity toward human fibroblasts and only revealed hemolytic activity at high concentrations. Thus, PEP-IA18 exhibited antifungal and anti-biofilm properties with potential applicability in the treatment of infections caused byCandidaspecies. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-12-10T20:04:30Z 2020-12-10T20:04:30Z 2020-07-02 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1080/08927014.2020.1776857 Biofouling. Abingdon: Taylor & Francis Ltd, 11 p., 2020. 0892-7014 http://hdl.handle.net/11449/197047 10.1080/08927014.2020.1776857 WOS:000546318700001 |
url |
http://dx.doi.org/10.1080/08927014.2020.1776857 http://hdl.handle.net/11449/197047 |
identifier_str_mv |
Biofouling. Abingdon: Taylor & Francis Ltd, 11 p., 2020. 0892-7014 10.1080/08927014.2020.1776857 WOS:000546318700001 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Biofouling |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
11 |
dc.publisher.none.fl_str_mv |
Taylor & Francis Ltd |
publisher.none.fl_str_mv |
Taylor & Francis Ltd |
dc.source.none.fl_str_mv |
Web of Science reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1799965754787889152 |