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Anti-infectious and anti-inflammatory effects of peptide fragments sequentially derived from the antimicrobial peptide centrocin 1 isolated from the green sea urchin, Strongylocentrotus droebachiensis

Camilla Björn1, Joakim Håkansson12, Emma Myhrman1, Veronika Sjöstrand1, Tor Haug3, Kerstin Lindgren1, Hans-Matti Blencke3, Klara Stensvåg3* and Margit Mahlapuu1*

Author Affiliations

1 Pergamum AB, Arvid Wallgrens Backe 20, 413 46, Gothenburg, Sweden

2 Present address: SP Technical Research Institute of Sweden, Medical Device Technology, Brinellgatan 4, 504 62, Borås, Sweden

3 Norwegian College of Fishery Science, Faculty of Biosciences, Fisheries and Economics, University of Tromsø, Tromsø N-9037, Norway

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AMB Express 2012, 2:67  doi:10.1186/2191-0855-2-67

Published: 13 December 2012


Bacterial resistance against antibiotic treatment has become a major threat to public health. Antimicrobial peptides (AMPs) have emerged as promising alternative agents for treatment of infectious diseases. This study characterizes novel synthetic peptides sequentially derived from the AMP centrocin 1, isolated from the green sea urchin, for their applicability as anti-infective agents.

The microbicidal effect of centrocin 1 heavy chain (CEN1 HC-Br), its debrominated analogue (CEN1 HC), the C-terminal truncated variants of both peptides, i.e. CEN1 HC-Br (1–20) and CEN1 HC (1–20), as well as the cysteine to serine substituted equivalent CEN1 HC (Ser) was evaluated using minimal microbicidal concentration assay. The anti-inflammatory properties were assessed by measuring the inhibition of secretion of pro-inflammatory cytokines. All the peptides tested exhibited marked microbicidal and anti-inflammatory properties. No difference in efficacy was seen comparing CEN1 HC-Br and CEN1 HC, while the brominated variant had higher cytotoxicity. C-terminal truncation of both peptides reduced salt-tolerability of the microbicidal effect as well as anti-inflammatory actions. Also, serine substitution of cysteine residue decreased the microbicidal effect. Thus, from the peptide variants tested, CEN1 HC showed the best efficacy and safety profile. Further, CEN1 HC significantly reduced bacterial counts in two different animal models of infected wounds, while Staphylococcus aureus and methicillin-resistant S. aureus (MRSA) failed to develop resistance against this peptide under continued selection pressure. In summary, CEN1 HC appears a promising new antimicrobial agent, and clinical studies are warranted to evaluate the applicability of this AMP for local treatment of infections in man.

Antibacterial peptide; Wound infection; Antibiotic resistance; MRSA