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JAC Advance Access originally published online on April 14, 2003
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Journal of Antimicrobial Chemotherapy (2003) 51, 1159-1165
© 2003 The British Society for Antimicrobial Chemotherapy

Enhancement of antibacterial and lipopolysaccharide binding activities of a human lactoferrin peptide fragment by the addition of acyl chain

Andreja Majerle, Jurka Kidric and Roman Jerala*

Laboratory of Biotechnology, National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia

Received 22 October 2002; returned 13 December 2002; revised 17 February 2003; 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

* Corresponding author. Tel: +386-1-476-0372; Fax: +386-1-476-0300; E-mail: roman.jerala{at}ki.si


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