Characterization and functional recovery of a novel antimicrobial peptide (CECdir-CECret) from inclusion bodies after expression in Escherichia coli

Schmitt, P.; Mercado L.; Diaz M.; Guzman, F; Arenas, G.; Marshall, SH

Abstract

CECdir-CECret is a novel non-toxic doublet 8.5 kDa peptide representing the natural coding sequence of the antimicrobial peptide Cecropin A from Drosophila melanogaster fused in-frame to its own inverted version. Expression of this cloned doublet peptide in Escherichia coli, yielded peptides that were mostly packaged into inclusion bodies. The new molecule was purified, solubilized and refolded, through a standard guanidine-based procedure. The recovered refolded peptides were then characterized by HPLC chromatography, MALDI-TOF-mass spectrometry and peptide sequencing, and finally evaluated for their antimicrobial potential. The novel doublet peptide CECdir-CECret, displays an enhanced in vitro antimicrobial activity and action spectrum in comparison to the monomer Cecropin A. © 2008 Elsevier Inc. All rights reserved.

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Título según WOS: Characterization and functional recovery of a novel antimicrobial peptide (CECdir-CECret) from inclusion bodies after expression in Escherichia coli
Título según SCOPUS: Characterization and functional recovery of a novel antimicrobial peptide (CECdir-CECret) from inclusion bodies after expression in Escherichia coli
Título de la Revista: PEPTIDES
Volumen: 29
Número: 4
Editorial: Elsevier Science Inc.
Fecha de publicación: 2008
Página de inicio: 512
Página final: 519
Idioma: English
URL: http://linkinghub.elsevier.com/retrieve/pii/S0196978107005293
DOI:

10.1016/j.peptides.2007.12.012

Notas: ISI, SCOPUS