Abstract
Mammalian defensins, a class of antibacterial peptides, are composed of 29–35 amino acids with six cysteines which form three disulfide bonds. Structural studies indicate a triple stranded β-sheet structure with a well defined β-hairpin loop at the C-terminal region. It is demonstrated in this report that 18 and 26 residue synthetic peptides corresponding to the β-hairpin region, constrained by a single disulfide bond, have potent antimicrobial activity without hemolytic activity. Circular dichroism spectroscopy indicates that the single S–S bridge appears to constrain the peptides to a β-structure. Peptides corresponding to the β-hairpin region of defensins could thus be attractive candidates as therapeutic agents as well as good model compounds for investigation of the various physiological actions of defensins.
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