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.
Keywords: Disulphide bond, refolding, recombinant expression, antimicrobial peptide, inclusion body
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