JAC Advance Access published online on April 14, 2003
Journal of Antimicrobial Chemotherapy, doi:10.1093/jac/dkg219
© 2003 by The British Society for Antimicrobial Chemotherapy
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Original article
1 Laboratory of Biotechnology, National Institute of Chemistry,
Hajdrihova 19, SI-1000 Ljubljana, Slovenia
* Corresponding author. E-mail: roman.jerala{at}ki.si.
Received 22 October 2002
; revised 13 December 2002
; accepted 18 February 2003
Cationic antibacterial peptides are potentially therapeutic
in the treatment of sepsis, because of their amalgamated antibacterial
and lipopolysaccharide-binding activities. We prepared acyl analogues
of the peptide fragment of human lactoferrin, which originally had
weak antibacterial activity. It was found that 12 carbon units constitute
the optimal acyl chain length, enhancing the antibacterial activity
and binding of lipopolysaccharide by up to two orders of magnitude. Lactoferrin-based
lipopeptides approached the activity of polymyxin B, a lipopeptide
of natural origin, but were also active against Gram-positive bacteria.
Keywords: antibacterial peptide, endotoxin, human lactoferrin,
lipopeptide
Enhancement of antibacterial and lipopolysaccharide binding
activities of a human lactoferrin peptide fragment by the addition
of acyl chain
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