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 α-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 α-helices contain antimicrobial activity, the pepti...

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Bibliographic Details
Published in:FEMS microbiology letters 1999-10, Vol.179 (2), p.217-222
Main Authors: Groenink, Jasper, Walgreen-Weterings, Els, van ’t Hof, Wim, Veerman, Enno C.I, Nieuw Amerongen, Arie V
Format: Article
Language:English
Subjects:
Antimicrobial peptide
Lactoferrin
Oral bacterium
Online Access:Get full text
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Summary:Peptides derived from the N-terminal domain that comprises an amphipathic α-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 α-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.
ISSN:0378-1097
1574-6968
DOI:10.1016/S0378-1097(99)00414-0