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 alpha-helix in human lactoferrin (LFh 18-31 and LFh 20-38) and bovine lactoferrin (LFb 17-30 and LFb 19-37) were chemically synthesised. Since many positively charged amphipathic alpha-helices contain antimicrobial activity, the peptides were tested for their antimicrobial activity against various oral pathogens. Both peptides from bovine lactoferrin had more potent antimicrobial activities than the human equivalents. Peptide LFb 17-30, containing the largest number of positively charged amino acids, showed the highest antimicrobial activity to both Gram-positive and Gram-negative bacteria. Since native lactoferrin molecules had no killing activity, release of these peptides from the native protein should be investigated to explore the use in oral care products.
Groenink
J
J
Department of Oral Biology, Section Oral Biochemistry, Academic Centre for Dentistry Amsterdam (ACTA), Van der Boechorststraat 7, 1081 BT, Amsterdam, The Netherlands. j.groenink.obc.acta@med.vu.nl
Walgreen-Weterings
E
E
van 't Hof
W
W
Veerman
E C
EC
Nieuw Amerongen
A V
AV
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001419:Bacteria / Q000187:drug effects*; D002417:Cattle; D006801:Humans; D007781:Lactoferrin / Q000494:pharmacology*; D008969:Molecular Sequence Data; D009055:Mouth / Q000382:microbiology*; D010446:Peptide Fragments / Q000494:pharmacology*
D000900:Anti-Bacterial Agents; D010446:Peptide Fragments; D007781:Lactoferrin