An antifungal peptide from passion fruit (Passiflora edulis) seeds with similarities to 2S albumin proteins
Autor(a) principal: | |
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Data de Publicação: | 2006 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UCB |
Texto Completo: | http://twingo.ucb.br:8080/jspui/handle/10869/676 https://repositorio.ucb.br:9443/jspui/handle/123456789/7806 |
Resumo: | An actual worldwide problem consists of an expressive increase of economic losses and health problems caused by fungi. In order to solve this problem, several studies have been concentrating on the screening of novel plant defence peptides with antifungal activities. These peptides are commonly characterized by having low molecular masses and cationic charges. This present work reports on the purification and characterization of a novel plant peptide of 5.0 kDa, Pe-AFP1, purified from the seeds of passion fruit (Passiflora edulis). Purification was achieved using a Red- Sepharose Cl-6B affinity column followed by reversed-phase chromatography on Vydac C18-TP column. In vitro assays indicated that Pe-AFP1 was able of inhibiting the development of the filamentous fungi Trichoderma harzianum, Fusarium oxysporum, and Aspergillus fumigatus with IC50 values of 32, 34, and 40 μg ml−1, respectively, but not of Rhyzoctonia solani, Paracoccidioides brasiliensis and Candida albicans. This protein was also subjected to automated N-terminal amino acid sequence, showing high degree of similarities to storage 2S albumins, adding a new member to this protein-defence family. The discovery of Pe-AFP1 could contribute, in a near future, to the development of biotechnological products as antifungal drugs and transgenic plants with enhanced resistance to pathogenic fungi. |
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Pelegrini, Patrícia BarbosaNoronha, Eliane FerreiraMuniz, Michele Aline RossiVasconcelos, Ilka MariaChiarello, Marileusa DosolinaOliveira, José Tadeu Abreu deFranco, Octavio Luiz2016-10-10T03:52:44Z2016-10-10T03:52:44Z2006PELEGRINI, Patricia et al. An antifungal peptide from passion fruit (Passiflora edulis) seeds with similarities to 2S-albumin proteins. Biochimica et Biophysica Acta, v. 1764, n. 6, p. 1141-1146, 2006.http://twingo.ucb.br:8080/jspui/handle/10869/676https://repositorio.ucb.br:9443/jspui/handle/123456789/7806An actual worldwide problem consists of an expressive increase of economic losses and health problems caused by fungi. In order to solve this problem, several studies have been concentrating on the screening of novel plant defence peptides with antifungal activities. These peptides are commonly characterized by having low molecular masses and cationic charges. This present work reports on the purification and characterization of a novel plant peptide of 5.0 kDa, Pe-AFP1, purified from the seeds of passion fruit (Passiflora edulis). Purification was achieved using a Red- Sepharose Cl-6B affinity column followed by reversed-phase chromatography on Vydac C18-TP column. In vitro assays indicated that Pe-AFP1 was able of inhibiting the development of the filamentous fungi Trichoderma harzianum, Fusarium oxysporum, and Aspergillus fumigatus with IC50 values of 32, 34, and 40 μg ml−1, respectively, but not of Rhyzoctonia solani, Paracoccidioides brasiliensis and Candida albicans. This protein was also subjected to automated N-terminal amino acid sequence, showing high degree of similarities to storage 2S albumins, adding a new member to this protein-defence family. The discovery of Pe-AFP1 could contribute, in a near future, to the development of biotechnological products as antifungal drugs and transgenic plants with enhanced resistance to pathogenic fungi.Made available in DSpace on 2016-10-10T03:52:44Z (GMT). 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de Publicaçõeshttps://repositorio.ucb.br:9443/jspui/ |
dc.title.pt_BR.fl_str_mv |
An antifungal peptide from passion fruit (Passiflora edulis) seeds with similarities to 2S albumin proteins |
title |
An antifungal peptide from passion fruit (Passiflora edulis) seeds with similarities to 2S albumin proteins |
spellingShingle |
An antifungal peptide from passion fruit (Passiflora edulis) seeds with similarities to 2S albumin proteins Pelegrini, Patrícia Barbosa Plant defence Antifungal Passiflora edulis Pe-AFP1 2S albumin Storage proteins |
title_short |
An antifungal peptide from passion fruit (Passiflora edulis) seeds with similarities to 2S albumin proteins |
title_full |
An antifungal peptide from passion fruit (Passiflora edulis) seeds with similarities to 2S albumin proteins |
title_fullStr |
An antifungal peptide from passion fruit (Passiflora edulis) seeds with similarities to 2S albumin proteins |
title_full_unstemmed |
An antifungal peptide from passion fruit (Passiflora edulis) seeds with similarities to 2S albumin proteins |
title_sort |
An antifungal peptide from passion fruit (Passiflora edulis) seeds with similarities to 2S albumin proteins |
author |
Pelegrini, Patrícia Barbosa |
author_facet |
Pelegrini, Patrícia Barbosa Noronha, Eliane Ferreira Muniz, Michele Aline Rossi Vasconcelos, Ilka Maria Chiarello, Marileusa Dosolina Oliveira, José Tadeu Abreu de Franco, Octavio Luiz |
author_role |
author |
author2 |
Noronha, Eliane Ferreira Muniz, Michele Aline Rossi Vasconcelos, Ilka Maria Chiarello, Marileusa Dosolina Oliveira, José Tadeu Abreu de Franco, Octavio Luiz |
author2_role |
author author author author author author |
dc.contributor.author.fl_str_mv |
Pelegrini, Patrícia Barbosa Noronha, Eliane Ferreira Muniz, Michele Aline Rossi Vasconcelos, Ilka Maria Chiarello, Marileusa Dosolina Oliveira, José Tadeu Abreu de Franco, Octavio Luiz |
dc.subject.por.fl_str_mv |
Plant defence Antifungal Passiflora edulis Pe-AFP1 2S albumin Storage proteins |
topic |
Plant defence Antifungal Passiflora edulis Pe-AFP1 2S albumin Storage proteins |
dc.description.abstract.por.fl_txt_mv |
An actual worldwide problem consists of an expressive increase of economic losses and health problems caused by fungi. In order to solve this problem, several studies have been concentrating on the screening of novel plant defence peptides with antifungal activities. These peptides are commonly characterized by having low molecular masses and cationic charges. This present work reports on the purification and characterization of a novel plant peptide of 5.0 kDa, Pe-AFP1, purified from the seeds of passion fruit (Passiflora edulis). Purification was achieved using a Red- Sepharose Cl-6B affinity column followed by reversed-phase chromatography on Vydac C18-TP column. In vitro assays indicated that Pe-AFP1 was able of inhibiting the development of the filamentous fungi Trichoderma harzianum, Fusarium oxysporum, and Aspergillus fumigatus with IC50 values of 32, 34, and 40 μg ml−1, respectively, but not of Rhyzoctonia solani, Paracoccidioides brasiliensis and Candida albicans. This protein was also subjected to automated N-terminal amino acid sequence, showing high degree of similarities to storage 2S albumins, adding a new member to this protein-defence family. The discovery of Pe-AFP1 could contribute, in a near future, to the development of biotechnological products as antifungal drugs and transgenic plants with enhanced resistance to pathogenic fungi. |
dc.description.status.pt_BR.fl_txt_mv |
Publicado |
description |
An actual worldwide problem consists of an expressive increase of economic losses and health problems caused by fungi. In order to solve this problem, several studies have been concentrating on the screening of novel plant defence peptides with antifungal activities. These peptides are commonly characterized by having low molecular masses and cationic charges. This present work reports on the purification and characterization of a novel plant peptide of 5.0 kDa, Pe-AFP1, purified from the seeds of passion fruit (Passiflora edulis). Purification was achieved using a Red- Sepharose Cl-6B affinity column followed by reversed-phase chromatography on Vydac C18-TP column. In vitro assays indicated that Pe-AFP1 was able of inhibiting the development of the filamentous fungi Trichoderma harzianum, Fusarium oxysporum, and Aspergillus fumigatus with IC50 values of 32, 34, and 40 μg ml−1, respectively, but not of Rhyzoctonia solani, Paracoccidioides brasiliensis and Candida albicans. This protein was also subjected to automated N-terminal amino acid sequence, showing high degree of similarities to storage 2S albumins, adding a new member to this protein-defence family. The discovery of Pe-AFP1 could contribute, in a near future, to the development of biotechnological products as antifungal drugs and transgenic plants with enhanced resistance to pathogenic fungi. |
publishDate |
2006 |
dc.date.issued.fl_str_mv |
2006 |
dc.date.accessioned.fl_str_mv |
2016-10-10T03:52:44Z |
dc.date.available.fl_str_mv |
2016-10-10T03:52:44Z |
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info:eu-repo/semantics/publishedVersion |
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info:eu-repo/semantics/article |
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publishedVersion |
format |
article |
dc.identifier.citation.fl_str_mv |
PELEGRINI, Patricia et al. An antifungal peptide from passion fruit (Passiflora edulis) seeds with similarities to 2S-albumin proteins. Biochimica et Biophysica Acta, v. 1764, n. 6, p. 1141-1146, 2006. |
dc.identifier.uri.fl_str_mv |
http://twingo.ucb.br:8080/jspui/handle/10869/676 https://repositorio.ucb.br:9443/jspui/handle/123456789/7806 |
identifier_str_mv |
PELEGRINI, Patricia et al. An antifungal peptide from passion fruit (Passiflora edulis) seeds with similarities to 2S-albumin proteins. Biochimica et Biophysica Acta, v. 1764, n. 6, p. 1141-1146, 2006. |
url |
http://twingo.ucb.br:8080/jspui/handle/10869/676 https://repositorio.ucb.br:9443/jspui/handle/123456789/7806 |
dc.language.iso.fl_str_mv |
eng |
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eng |
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openAccess |
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UCB |
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UCB |
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Repositório Institucional da UCB |
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Repositório Institucional da UCB |
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