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LEAP‐1, a novel highly disulfide‐bonded human peptide, exhibits antimicrobial activity
Author(s) -
Krause Alexander,
Neitz Susanne,
Mägert Hans-Jürgen,
Schulz Axel,
Forssmann Wolf-Georg,
Schulz-Knappe Peter,
Adermann Knut
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01920-7
Subject(s) - micrococcus luteus , peptide , bacillus subtilis , antimicrobial , antimicrobial peptides , biochemistry , bacillus megaterium , cysteine , chemistry , microbiology and biotechnology , peptide sequence , yeast , biology , bacteria , enzyme , escherichia coli , gene , genetics
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.