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Antimicrob Agents Chemother. 1985 May; 27(5): 836-840

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 and H Brandis

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.

Antimicrob Agents Chemother. 1985 May; 27(5): 836-840




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