Cationic amphipathic peptides, derived from bovine and human lactoferrins,with antimicrobial activity against oral pathogens

Peptides derived from the N-terminal domain that comprises an amphipathic a lpha-helix in human lactoferrin (LFh 18-31 and LFh 20-38) and bovine lactof errin (LFb 17-30 and LFb 19-37) were chemically synthesised. Since many pos itively charged amphipathic alpha-helices contain antimicrobial activity, t he peptides were tested for their antimicrobial activity against various or al pathogens. Both peptides from bovine lactoferrin had more potent antimic robial activities than the human equivalents. Peptide LFb 17-30, containing the largest number of positively charged amino acids, showed the highest a ntimicrobial activity to both Gram-positive and Gram-negative bacteria. Sin ce native lactoferrin molecules had no killing activity, release of these p eptides from the native protein should be investigated to explore the use i n oral care products. (C) 1999 Federation of European Microbiological Socie ties. Published by Elsevier Science B.V. All rights reserved.