Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/24301

TitleRecombinant expression and purification of the antimicrobial peptide Magainin-2
Author(s)Ramos, Reinaldo Rodrigues
Moreira, Susana Margarida Gomes
Rodrigues, Ana Cristina Costa
Gama, F. M.
Domingues, Lucília
KeywordsMagainin-2
Recombinant protein
Antimicrobial peptide
Issue date2013
PublisherAmerican Institute of Chemical Engineers (AIChE)
JournalBiotechnology progress
Abstract(s)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.
TypeArticle
URIhttp://hdl.handle.net/1822/24301
DOI10.1002/btpr.1650
ISSN8756-7938
e-ISSN1520-6033
Publisher versionhttp://dx.doi.org/10.1002/btpr.1650
Peer-Reviewedyes
AccessOpen access
Appears in Collections:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

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