Production of Cell-Penetrating Peptides in Escherichia coli Using an Intein-Mediated System
Author
dc.contributor.author
Rodríguez Gallardo, Vida
Author
dc.contributor.author
Lascani Monsalve, Jorge
Author
dc.contributor.author
Asenjo de Leuze, Juan
Author
dc.contributor.author
Andrews Farrow, Bárbara
Admission date
dc.date.accessioned
2015-08-23T00:12:57Z
Available date
dc.date.available
2015-08-23T00:12:57Z
Publication date
dc.date.issued
2015
Cita de ítem
dc.identifier.citation
Appl Biochem Biotechnol (2015) 175:3025–3037
en_US
Identifier
dc.identifier.issn
0273-2289
Identifier
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DOI: 10.1007/s12010-015-1484-7
Identifier
dc.identifier.uri
https://repositorio.uchile.cl/handle/2250/133041
General note
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Artículo de publicación ISI
en_US
Abstract
dc.description.abstract
Cell-penetrating peptides are molecules with the ability to cross membranes and
enter cells. Attention has been put on these peptides as a tool for drug delivery research, as they
are able to serve as delivery vectors for large molecules. Intracellular delivery of bioactive
peptides is a very promising research area for clinical applications, since peptides are able to
simulate protein regions and thus modulate key intracellular protein-protein interactions.
Therefore, evaluation of different strategies for production of these peptides is necessary. In
this work, an intein-mediated system was used to evaluate Escherichia coli recombinant
production of p53pAnt and PNC27 anticancer cell-penetrating peptides. It was demonstrated
that the pTXB1 and the pTYB11 vector systems are suitable for production of this kind of
peptides. The production process involves a low-temperature induction process and an efficient
on-column intein-mediated cleavage, which allowed an effective peptide recovery using
a single chromatographic step.