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

FEBS Letters - Tập 480 Số 2-3 - Trang 147-150 - 2000
Alexander Krause1, Susanne Neitz, Hans‐Jürgen Mägert, Axel Schulz, Wolf Georg Forssmann, Peter Schulz‐Knappe, A. Frimpong–Boateng
1Niedersächsisches Institut für Peptid-Forschung, Hannover, Germany

Tóm tắt

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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FEBS Letters

Tập 480 Số 2-3

147-150

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