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Recombinant production of antimicrobial peptides in Escherichia coli: a review.
- Source :
-
Protein expression and purification [Protein Expr Purif] 2011 Dec; Vol. 80 (2), pp. 260-7. Date of Electronic Publication: 2011 Aug 06. - Publication Year :
- 2011
-
Abstract
- Antimicrobial peptides are of great interest due to their potential application as novel antibiotics. Large quantities of highly purified peptides are required to meet the needs of basic research and clinical trials. Compared with isolation from natural sources and chemical synthesis, recombinant approach offers the most cost-effective means for large-scale peptide manufacture. Among the systems available for heterologous protein production, Escherichia coli has been the most widely used host. Antimicrobial peptides produced in E. coli are often expressed as fusion proteins, a strategy necessary to mask these peptides' lethal effect towards the host and protect them from proteolytic degradation. The present article reviews commonly used fusion partners (e.g., solubility-enhancing, aggregation-promoting and self-cleavable carriers, etc.), cleavage methods and optimization options for antimicrobial peptides production in E. coli. In addition, the various approaches developed to generate recombinant human antimicrobial peptide LL-37, which offer excellent examples demonstrating effective production strategies, were briefly discussed.<br /> (Copyright © 2011 Elsevier Inc. All rights reserved.)
- Subjects :
- Antimicrobial Cationic Peptides genetics
Antimicrobial Cationic Peptides metabolism
Carrier Proteins genetics
Carrier Proteins metabolism
Cathelicidins genetics
Cathelicidins isolation & purification
Cathelicidins metabolism
Escherichia coli genetics
Histidine metabolism
Humans
Inclusion Bodies metabolism
Peptide Hydrolases metabolism
Protein Multimerization
Protein Refolding
Protein Sorting Signals
Recombinant Proteins genetics
Recombinant Proteins metabolism
Solubility
Thioredoxins metabolism
Antimicrobial Cationic Peptides isolation & purification
Escherichia coli metabolism
Recombinant Proteins isolation & purification
Subjects
Details
- Language :
- English
- ISSN :
- 1096-0279
- Volume :
- 80
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Protein expression and purification
- Publication Type :
- Academic Journal
- Accession number :
- 21843642
- Full Text :
- https://doi.org/10.1016/j.pep.2011.08.001