Structural similarities of the staphylococcin-like peptide Pep-5 to the peptide antibiotic nisin

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Abstract
The staphylococcin-like peptide Pep-5 [an antibacterial drug produced by Staphylococcus epidermidis 5] is a complex mixture of closely related and strongly basic peptides. Five peptides were purified by high-pressure liquid chromatography on reversed-phase and gel filtration columns and further characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and amino acid analysis. Four peptides have MW of .apprx. 3500, whereas one is of double size. All contain the thioether amino acid lanthionine and a large number of Lys residues per molecule. The amino terminus of the main active peptide is blocked; the carboxy-terminal end is formed by a Lys residue. The data obtained for Pep-5 suggest striking structural similarities to the peptide antibiotics nisin and subtilin.