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Characterization and functional recovery of a novel antimicrobial peptide (CEC dir-CEC ret) from inclusion bodies after expression in Escherichia coli
Keywords: sequence, acid, performance, proteins, chromatography, peptides, animals, expression, protein, cell, drosophila, matrix, liquid, mass, agents, laser, time, melanogaster, vitro, fusion, antimicrobial, bodies, agent, inclusion, flight, coli, drug, article, desorption, recombinant, ionization, spectrometry, polypeptide, activity, assisted, antibiotic, controlled, cecropin, study, amino, priority, of, in, nonhuman, journal, circular, dichroism, a, Escherichia, High, Spectrometry,, unclassified, Anti-Infective, Mass,, Cationic, Matrix-Assisted, Desorption-Ionization, cec
Abstract
CEC dir-CEC ret 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 CEC dir-CEC ret, displays an enhanced in vitro antimicrobial activity and action spectrum in comparison to the monomer Cecropin A. © 2008 Elsevier Inc. All rights reserved.
Más información
| Título de la Revista: | PEPTIDES |
| Volumen: | 29 |
| Número: | 4 |
| Editorial: | Elsevier Science Inc. |
| Fecha de publicación: | 2008 |
| Página de inicio: | 512 |
| Página final: | 519 |
| URL: | http://www.scopus.com/inward/record.url?eid=2-s2.0-40249083999&partnerID=q2rCbXpz |