Sabiia Seb
PortuguêsEspañolEnglish
Embrapa
        Busca avançada

Botão Atualizar


Botão Atualizar

Ordenar por: 

RelevânciaAutorTítuloAnoImprime registros no formato resumido
Registros recuperados: 5
Primeira ... 1 ... Última
Imagem não selecionada

Imprime registro no formato completo
Intein-mediated expression of cecropin in Escherichia coli Electron. J. Biotechnol.
Díaz,Mauricio; Venturini,Elena; Marchetti,Stefano; Arenas,Gloria; Marshall,Sergio H.
Different strategies have been used to overcome the difficulties to produce antimicrobial peptides. Here we used Intein Mediated Purification with an Affinity Chitin-binding Tag (IMPACT-System, New England Biolabs) for the expression of the antimicrobial peptide cecropin to reduce its sensitivity to intracellular proteases and use its inducible self-cleaving capability to remove the carrier. Cecropin was cloned into suitable expression vector pTYB11, and expression induced by IPTG in Escherichia coli ER2566. The use of 22ºC induction allowed the expression of cecropin with its intein carrier in soluble form. Cell extracts were purified by chitin affinity chromatography and intein-mediated splicing of the target protein was achieved by thiol addition,...
Tipo: Journal article Palavras-chave: Antimicrobial; Cecropin; Fusion; Intein; Peptide; Soluble.
Ano: 2012 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582012000200003
Imagem não selecionada

Imprime registro no formato completo
Design and expression of a retro doublet of cecropin with enhanced activity Electron. J. Biotechnol.
Díaz,Mauricio; Arenas,Gloria; Marshall,Sergio H.
Novel doublet molecules of cecropin A from Drosophila melanogaster were designed and constructed combining the regular (CECdir) with the inverted (CECret) coding sequence of the standard CEC A1 gene resulting in the following configurations: CECdir-CECret and CECret-CECdir. These two recombinant molecules were generated using a three-primer driven PCR reaction yielding composite single functional aminoacidic molecules with the coding sequences of CECdir linked in frame with the coding sequence of CECret and vice versa. In order to obtain these constructions, a retropeptide DNA-coding sequence was chemically synthesized to match the expected polarity of the newly generated CECret sequence. Both doublet antimicrobial peptides (drAMPs) were cloned in the T7...
Tipo: Journal article Palavras-chave: Antimicrobial peptides; Escherichia coli; Expression.
Ano: 2008 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582008000200006
Imagem não selecionada

Imprime registro no formato completo
Gill tissues of the mussel Mytilus edulis chilensis: A new source for antimicrobial peptides Electron. J. Biotechnol.
Mercado,Luis; Schmitt,Paulina; Marshall,Sergio H; Arenas,Gloria.
Antimicrobial peptides are small-sized, cationic and amphipathic molecules able to neutralize pathogenic microorganisms. Their antimicrobial effects tie them to mechanisms of immune defense, which is why they have been normally purified from immune cells. We describe an apparently new group of antimicrobial peptides from gill tissues of the mussel Mytilus edulis chilensis. 20 specimens yielded 40 g of gills which produced 16 mg of an enriched fraction with antimicrobial activity as low as 0.045 µg/µl over reference strains. Considering the chemical nature of these molecules we used an acid extraction procedure followed by consecutive cationic exchange and hydrophobic interaction chromatography steps for peptide enrichment. The resulting...
Tipo: Journal article Palavras-chave: Antimicrobial peptides; Biochemical characterization; Gill tissues; In vitro activity; Mussels.
Ano: 2005 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582005000300008
Imagem não selecionada

Imprime registro no formato completo
Protective effect of an antimicrobial peptide from Mytilus edulis chilensis expressed in Nicotiana tabacum L. Electron. J. Biotechnol.
Arenas,Gloria; Marshall,Sergio H.; Espinoza,Valeria; Ramírez,Ingrid; Peña-Cortés,Hugo.
A "defensin-like" antibacterial peptide from Mytilus edulis chilensis, was sub-cloned into a binary vector for expression in plant tissues. The resulting new clone was electroporated into A. tumefaciens to transform tobacco plants. The presence of the construct in transgenic tobacco lines was demonstrated through RT-PCR, Northern and Western blots. Transformed positive plants were selected and grown for challenging. Tobacco leaves were infiltrated with Pseudomonassyringae pv. syringae and visual lesions determined at different times post-exposure. Of seven plants exposed, four gave variable protection up to seven days post-infection while one of them appears to be fully protected. These results suggest that defensin-like antimicrobial peptides from...
Tipo: Journal article Palavras-chave: Antibacterial peptide; Disease resistance; In vivo expression; Nicotiana tabacum L.; Pseudomonassyringae pv. syringae; Transgenic tobacco plants.
Ano: 2006 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582006000200008
Imagem não selecionada

Imprime registro no formato completo
Antimicrobial peptides: A natural alternative to chemical antibiotics and a potential for applied biotechnology Electron. J. Biotechnol.
Marshall,Sergio H.; Arenas,Gloria.
A large group of low molecular weight natural compounds that exhibit antimicrobial activity has been isolated from animals and plants during the past two decades. Among them, cationic peptides are the most widespread. Interestingly, the variety and diversity of these peptides seem to be much wider than suspected. In fact, novel classes of peptides with varying chemical propertiescontinue to be isolated from different vertebrate and invertebrate species, as well as from bacteria. To the early characterized peptides, mostly cationic in nature, anionic peptides, aromatic dipeptides, processed forms of oxygen-binding proteins and processed forms of natural structural and functional proteins can now be added, just to name a few. In spite of the astonishing...
Tipo: Journal article
Ano: 2003 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582003000300011
Registros recuperados: 5
Primeira ... 1 ... Última
 

Empresa Brasileira de Pesquisa Agropecuária - Embrapa
Todos os direitos reservados, conforme Lei n° 9.610
Política de Privacidade
Área restrita

Embrapa
Parque Estação Biológica - PqEB s/n°
Brasília, DF - Brasil - CEP 70770-901
Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco

Valid HTML 4.01 Transitional