Use of magnetic carboxyl beads to purify a cationic peptide in a batch system
| Autor: | Fabrice Bayard, Aurélie Letourneau, Charlotte Cabanne, Gilles Joucla, Caroline Barbot, Bertrand Garbay, Amélie Raveneau |
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| Rok vydání: | 2009 |
| Předmět: |
chemistry.chemical_classification
Chromatography Antimicrobial peptides Ion chromatography Size-exclusion chromatography Biophysics Cationic polymerization Peptide Cell Biology medicine.disease_cause Models Biological Biochemistry Fusion protein law.invention Magnetics chemistry law Escherichia coli medicine Recombinant DNA Molecular Biology Antimicrobial Cationic Peptides |
| Zdroj: | Analytical Biochemistry. 384:350-352 |
| ISSN: | 0003-2697 |
| DOI: | 10.1016/j.ab.2008.10.016 |
| Popis: | Antimicrobial peptides (AMPs) are cationic molecules that are good leads for new antiinfective drugs. To obtain sufficient amounts, recombinant AMPs are generally produced as fusion proteins in Escherichia coli. Fusion partners facilitate purification of recombinant proteins. Fusion proteins are then cleaved by specific proteases, and cationic peptides are purified by size exclusion chromatography or ion exchange chromatography, neither of which is easily applicable to small volumes of diluted peptide samples. We developed a small-scale system that is easily adaptable for high-throughput screening and uses carboxyl magnetic beads to purify a cationic peptide from its fusion partner. |
| Databáze: | OpenAIRE |
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