Recombinant expression and purification of the antimicrobial peptide Magainin-2
Autor(a) principal: | |
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Data de Publicação: | 2013 |
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/1822/24301 |
Resumo: | Magainin-2 (MAG2) is a polycationic antimicrobial peptide isolated from the skin of the African clawed frog Xenopus laevis. It has a wide spectrum of antimicrobial activities against Gram-positive and Gram-negative bacteria, fungi and induces osmotic lysis of protozoa. MAG2 also possesses antiviral and antitumoral properties. These activities make this peptide a promising candidate for therapeutic applications. Recombinant expression systems are necessary for the affordable production of large amounts of the biologically active peptide. In this work, MAG2 has been cloned to the N-terminal of a family III carbohydrate-binding module fused to the linker sequence (LK-CBM3) from Clostridium thermocellum; a formic acid recognition site was introduced between the two modules for chemical cleavage of the peptide. The recombinant protein MAG2-LK-CBM3 was expressed in Escherichia coli BL21 (DE3) and MAG2 was successfully cleaved and purified from the fusion partner LK-CBM3. Its functionality was confirmed by testing its activity against Gram-negative bacteria. |
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Recombinant expression and purification of the antimicrobial peptide Magainin-2Magainin-2Recombinant proteinAntimicrobial peptideScience & TechnologyMagainin-2 (MAG2) is a polycationic antimicrobial peptide isolated from the skin of the African clawed frog Xenopus laevis. It has a wide spectrum of antimicrobial activities against Gram-positive and Gram-negative bacteria, fungi and induces osmotic lysis of protozoa. MAG2 also possesses antiviral and antitumoral properties. These activities make this peptide a promising candidate for therapeutic applications. Recombinant expression systems are necessary for the affordable production of large amounts of the biologically active peptide. In this work, MAG2 has been cloned to the N-terminal of a family III carbohydrate-binding module fused to the linker sequence (LK-CBM3) from Clostridium thermocellum; a formic acid recognition site was introduced between the two modules for chemical cleavage of the peptide. The recombinant protein MAG2-LK-CBM3 was expressed in Escherichia coli BL21 (DE3) and MAG2 was successfully cleaved and purified from the fusion partner LK-CBM3. Its functionality was confirmed by testing its activity against Gram-negative bacteria.American Institute of Chemical Engineers (AIChE)American Chemical SocietyUniversidade do MinhoRamos, Reinaldo RodriguesMoreira, Susana Margarida GomesRodrigues, Ana Cristina CostaGama, F. M.Domingues, Lucília20132013-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/24301eng8756-79381520-603310.1002/btpr.165023125137http://dx.doi.org/10.1002/btpr.1650info: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:RCAAP2023-07-21T12:44:43Zoai:repositorium.sdum.uminho.pt:1822/24301Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:42:27.633785Repositório 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 |
Recombinant expression and purification of the antimicrobial peptide Magainin-2 |
title |
Recombinant expression and purification of the antimicrobial peptide Magainin-2 |
spellingShingle |
Recombinant expression and purification of the antimicrobial peptide Magainin-2 Ramos, Reinaldo Rodrigues Magainin-2 Recombinant protein Antimicrobial peptide Science & Technology |
title_short |
Recombinant expression and purification of the antimicrobial peptide Magainin-2 |
title_full |
Recombinant expression and purification of the antimicrobial peptide Magainin-2 |
title_fullStr |
Recombinant expression and purification of the antimicrobial peptide Magainin-2 |
title_full_unstemmed |
Recombinant expression and purification of the antimicrobial peptide Magainin-2 |
title_sort |
Recombinant expression and purification of the antimicrobial peptide Magainin-2 |
author |
Ramos, Reinaldo Rodrigues |
author_facet |
Ramos, Reinaldo Rodrigues Moreira, Susana Margarida Gomes Rodrigues, Ana Cristina Costa Gama, F. M. Domingues, Lucília |
author_role |
author |
author2 |
Moreira, Susana Margarida Gomes Rodrigues, Ana Cristina Costa Gama, F. M. Domingues, Lucília |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Ramos, Reinaldo Rodrigues Moreira, Susana Margarida Gomes Rodrigues, Ana Cristina Costa Gama, F. M. Domingues, Lucília |
dc.subject.por.fl_str_mv |
Magainin-2 Recombinant protein Antimicrobial peptide Science & Technology |
topic |
Magainin-2 Recombinant protein Antimicrobial peptide Science & Technology |
description |
Magainin-2 (MAG2) is a polycationic antimicrobial peptide isolated from the skin of the African clawed frog Xenopus laevis. It has a wide spectrum of antimicrobial activities against Gram-positive and Gram-negative bacteria, fungi and induces osmotic lysis of protozoa. MAG2 also possesses antiviral and antitumoral properties. These activities make this peptide a promising candidate for therapeutic applications. Recombinant expression systems are necessary for the affordable production of large amounts of the biologically active peptide. In this work, MAG2 has been cloned to the N-terminal of a family III carbohydrate-binding module fused to the linker sequence (LK-CBM3) from Clostridium thermocellum; a formic acid recognition site was introduced between the two modules for chemical cleavage of the peptide. The recombinant protein MAG2-LK-CBM3 was expressed in Escherichia coli BL21 (DE3) and MAG2 was successfully cleaved and purified from the fusion partner LK-CBM3. Its functionality was confirmed by testing its activity against Gram-negative bacteria. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013 2013-01-01T00:00:00Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/1822/24301 |
url |
http://hdl.handle.net/1822/24301 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
8756-7938 1520-6033 10.1002/btpr.1650 23125137 http://dx.doi.org/10.1002/btpr.1650 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
American Institute of Chemical Engineers (AIChE) American Chemical Society |
publisher.none.fl_str_mv |
American Institute of Chemical Engineers (AIChE) American Chemical Society |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799132977445208064 |