Strategies for Recombinant Expression of Small, Highly Disulphide- Bonded, Cationic Antimicrobial Peptides

Title: Strategies for Recombinant Expression of Small, Highly Disulphide- Bonded, Cationic Antimicrobial Peptides

Volume: 15 Issue: 9

Author(s): A. L. Greenshields, L. C. Knickle, R. Syvitski and S. E. Douglas

Affiliation:

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

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.

Cite this article as:

Greenshields L. A., Knickle C. L., Syvitski R. and Douglas E. S., Strategies for Recombinant Expression of Small, Highly Disulphide- Bonded, Cationic Antimicrobial Peptides, Protein & Peptide Letters 2008; 15 (9) . https://dx.doi.org/10.2174/092986608785849281