LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity.
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Krause A, Neitz S, Magert HJ, Schulz A, Forssmann WG, Schulz-Knappe P, Adermann K
LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity.
FEBS Lett. 2000 Sep 1;480(2-3):147-50. doi: 10.1016/s0014-5793(00)01920-7.
- PubMed ID
- 11034317 [ View in PubMed]
- Abstract
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.