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

@article{Krause2000LEAP1AN,
  title={LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity.},
  author={Alexander Krause and Susanne Neitz and H J M{\"a}gert and Axel Schulz and Wolf Georg Forssmann and Peter Schulz-Knappe and Knut Adermann},
  journal={FEBS letters},
  year={2000},
  volume={480 2-3},
  pages={
          147-50
        }
}
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… CONTINUE READING
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