An antifungal peptide from passion fruit (Passiflora edulis) seeds with similarities to 2S albumin proteins

Detalhes bibliográficos
Autor(a) principal: Pelegrini, Patrícia Barbosa
Data de Publicação: 2006
Outros Autores: Noronha, Eliane Ferreira, Muniz, Michele Aline Rossi, Vasconcelos, Ilka Maria, Chiarello, Marileusa Dosolina, Oliveira, José Tadeu Abreu de, Franco, Octavio Luiz
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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spelling 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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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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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
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