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Home List of Titles Anti-microbial action of melanocortin peptides and identification of a novel X-Pro-d/l-Val sequence in Gram-positive and Gram-negative bacteria
Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/231205
- Anti-microbial action of melanocortin peptides and identification of a novel X-Pro-d/l-Val sequence in Gram-positive and Gram-negative bacteria
- Charnley, Mirren; Moir, Arthur J. G.; Douglas, C. W. Ian; Haycock, John W.
- The melanocortin peptides α-MSH, Lys-Pro-Val and Lys-Pro-d-Val are known to be potent anti-inflammatory agents; however their role as antibacterial peptides is less clear. The aim of this study was to determine whether these peptides displayed antibacterial properties, and specifically whether the Lys-Pro-d-Val tripeptide was more potent than Lys-Pro-Val, consistent with their anti-inflammatory actions. α-MSH, Ac-Lys-Pro-d-Val-NH2 and Ac-Lys-Pro-Val-NH2 were found to be antibacterial against both Gram-positive and Gram-negative bacteria (Staphylococcus aureus and Escherichia coli) over a broad range of concentrations compared to a control peptide, Ac-Ala-Ala-Ala-NH2. However, the relative potency of α-MSH, Ac-Lys-Pro-d-Val-NH2, Ac-Lys-Pro-Val-NH2 did not differ. Furthermore, it was found that the cationic charge on the lysine residue was not required for activity as a variant peptide Ac-Ala-Pro-d-Val-NH2 was also antibacterial. We therefore describe a novel X-Pro-d/l-Val peptide sequence with similarity to the short melanocortin peptides, which possess antibacterial activity. The combined anti-inflammatory and antibacterial action of such peptides may also have potential value therapeutically.
- Publication type
- Journal article
- Peptides, Vol. 29, no. 6 (Jun 2008), pp. 1004-1009
- Publication year
- FOR Code(s)
- 0304 Medicinal and Biomolecular Chemistry; 0606 Physiology; 1115 Pharmacology and Pharmaceutical Sciences
- Anti-microbial peptides; E. coli; Escherichia coli; Golden staph; Melanocortin peptides; Staphylococcus aureus
- Publisher URL
- Copyright © 2008 Elsevier Inc. All rights reserved.
- Additional information
- Supported by the UK Biotechnology and Biological Sciences Research Council (BBSRC).
- Peer reviewed