Antimicrobial Fusion Peptides

Jun 6, 2012 | Contact Author | By: Rachel Grabenhofer
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Title: Antimicrobial Fusion Peptides
  • Article

As reported by the technology license firm Ploughshare Innovations, antimicrobial peptides have been isolated from sources such as plants, amphibians, insects and microorganisms but have not been developed as antimicrobial agents because there are often disadvantages associated with their activity; such as toxic and haemolytic effects. To address these issues, Defense Science and Technology Laboratory (DSTL) scientists in the UK have engineered antimicrobial peptides based on the human peptide LL-37. DSTL is the center of scientific excellence for the UK Ministry of Defense.

Antimicrobial fusion peptides result from joining different peptides to form a new polypeptide with properties that may be different from the original peptides. This approach significantly increases the effectiveness of antimicrobial peptides and may reduce toxicity. In addition, the fusion structure is often more stable against proteases than the constituent peptides alone.

In this case, the LL-37 peptide was fused with another bioactive peptide or active fragment such that part or all of the resulting amino acid sequence was predicted to form an alpha-helix structure for the disruption of pathogen cell membranes. The fusion peptides described may be particularly useful against S. aureus and/or B. cepacia and/or Y. pseudotuberculosis infections, as well as athlete's foot, onychomycosis, Candida albicans, etc., in a variety of powders, creams etc.