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. 1985 May;27(5):836–840. doi: 10.1128/aac.27.5.836

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

H G Sahl, M Grossgarten, W R Widger, W A Cramer, H Brandis
PMCID: PMC180162  PMID: 4015073

Abstract

The staphylococcin-like peptide Pep-5 was shown to be 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 molecular weights of ca. 3,500, whereas one is of double size. All contain the thioether amino acid lanthionine and a large number of lysine residues per molecule. The amino terminus of the main active peptide is blocked; the carboxy-terminal end is formed by a lysine residue. The data obtained for Pep-5 suggest striking structural similarities to the peptide antibiotics nisin and subtilin.

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Selected References

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