| Literature DB >> 15062998 |
Marieke I A van der Kraan1, Jasper Groenink, Kamran Nazmi, Enno C I Veerman, Jan G M Bolscher, Arie V Nieuw Amerongen.
Abstract
The antimicrobial activity of bovine lactoferrin is attributed to lactoferricin, situated in the N1-domain. Based on common features of antimicrobial peptides, a second putative antimicrobial domain was identified in the N1-domain of lactoferrin, designated lactoferrampin. This novel peptide exhibited candidacidal activity, which was substantially higher than the activity of lactoferrin. Furthermore, lactoferrampin was active against Bacillus subtilis, Escherichia coli, and Pseudomonas aeruginosa, but not against the fermenting bacteria Actinomyces naeslundii, Porphyromonas gingivalis, Streptococcus mutans and Streptococcus sanguis. Notably, lactoferrampin is located in the N1-domain in close proximity to lactoferricin, which plays a crucial role in membrane-mediated activities of lactoferrin.Entities:
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Year: 2004 PMID： 15062998 DOI： 10.1016/j.peptides.2003.12.006
Source DB: PubMed Journal: Peptides ISSN： 0196-9781 Impact factor: 3.750