Abstract
Expression of two recombinant hepcidin homologues from Atlantic salmon, Salmo salar, characterization of their antimicrobial activity, and partial structural determination of the peptides is described. Expression was attempted in baculovirus and bacterial expression systems and the various purification and refolding methods used to determine the optimal strategy for production of active, correctly refolded hepcidin are reviewed.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antimicrobial Cationic Peptides / biosynthesis
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Antimicrobial Cationic Peptides / chemistry*
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Antimicrobial Cationic Peptides / isolation & purification
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Antimicrobial Cationic Peptides / pharmacology*
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Baculoviridae / genetics
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Chromatography, Affinity
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Cloning, Molecular
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Electrophoresis, Polyacrylamide Gel
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Endopeptidases / metabolism
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Escherichia coli / genetics
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Gram-Negative Bacteria / drug effects
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Gram-Positive Bacteria / drug effects
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Hepcidins
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Inclusion Bodies / metabolism
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Models, Molecular
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Nuclear Magnetic Resonance, Biomolecular
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Protein Folding
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / pharmacology
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Salmo salar
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Substances
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Antimicrobial Cationic Peptides
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Hepcidins
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Recombinant Proteins
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Endopeptidases
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TEV protease