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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity.

We report the isolation and characterization of a novel human peptide with antimicrobial activity, termed LEAP-1 (liver-expressed antimicrobial peptide). Using a mass spectrometric assay detecting cysteine-rich peptides, a 25-residue peptide containing four disulfide bonds was identified in human blood ultrafiltrate. LEAP-1 expression was predominantly detected in the liver, and, to a much lower extent, in the heart. In radial diffusion assays, Gram-positive Bacillus megaterium, Bacillus subtilis, Micrococcus luteus, Staphylococcus carnosus, and Gram-negative Neisseria cinerea as well as the yeast Saccharomyces cerevisiae dose-dependently exhibited sensitivity upon treatment with synthetic LEAP-1. The discovery of LEAP-1 extends the known families of mammalian peptides with antimicrobial activity by its novel disulfide motif and distinct expression pattern.[1]

References

  1. LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity. Krause, A., Neitz, S., Mägert, H.J., Schulz, A., Forssmann, W.G., Schulz-Knappe, P., Adermann, K. FEBS Lett. (2000) [Pubmed]
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