Strategies for Recombinant Expression of Small, Highly Disulphide- Bonded, Cationic Antimicrobial Peptides
Authors: Greenshields, A. L.; Knickle, L. C.; Syvitski, R.; Douglas, S. E.
Source: Protein and Peptide Letters, Volume 15, Number 9, September 2008 , pp. 985-994(10)
Publisher: Bentham Science Publishers
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.
Document Type: Research Article
Publication date: September 1, 2008
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.