Reduction in the bactericidal activity of selected cathelicidin peptides by bovine calf serum or exogenous endotoxin.

Synthetic cathelicidin peptides exhibit enhanced antimicrobial action and avid binding to LPS, thereby detoxifying the action of endotoxin released from degrading bacteria. A series of cathelicidin antimicrobial peptide (CAP) and sheep myeloid antimicrobial peptide (SMAP) congeners were examined to determine whether LPS-binding could predict other beneficial characteristics of the peptides. The peptides were challenged in complex media with bovine calf serum or LPS, and their ability to kill the Gram negative pathogens Klebsiella pneumoniae (ATCC 43816) or Pseudomonas aeruginosa (PA103) was then assessed. LPS-binding efficiency was not correlated with antimicrobial activity in complex media. Additionally, LPS- and serum-binding may interfere with the antimicrobial activity of peptides in complex media. Copyright 2004 Elsevier B.V.