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

      Febs Letters

      drug effects, Anti-Bacterial Agents, Anti-Infective Agents, classification, pharmacology, Antimicrobial Cationic Peptides, Bacillus megaterium, Bacillus subtilis, Base Sequence, DNA, Complementary, Disulfides, Hepcidins, Humans, Microbial Sensitivity Tests, Micrococcus luteus, Amino Acid Sequence, Molecular Sequence Data, Neisseria, Peptides, genetics, Proteins, Saccharomyces cerevisiae, Sequence Analysis, DNA, Staphylococcus

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          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.

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          11034317

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