Lactoferrampin: a novel antimicrobial peptide in the N1-domain of bovine lactoferrin

Peptides. 2004 Feb;25(2):177-83. doi: 10.1016/j.peptides.2003.12.006.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anti-Infective Agents / chemistry*
  • Cattle
  • Lactoferrin / chemistry*
  • Microbial Sensitivity Tests
  • Milk / chemistry*
  • Molecular Sequence Data
  • Peptide Fragments / chemistry*


  • Anti-Infective Agents
  • Peptide Fragments
  • Lactoferrin