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

FEBS Letters

Adermann, Knut¹  Mägert, Hans-Jürgen¹  Neitz, Susanne¹  Forssmann, Wolf-Georg¹  Schulz, Axel¹  Krause, Alexander¹  Schulz-Knappe, Peter¹ 

[1] Niedersächsisches Institut für Peptid-Forschung (IPF), Feodor-Lynen-Strasse 31, D-30625 Hannover, Germany

关键词: Antimicrobial peptide;    Liver;    Hemofiltrate;    Cysteine-rich peptide;   

DOI  :  10.1016/S0014-5793(00)01920-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown