Open AccessStructural similarities of the staphylococcin-like peptide Pep-5 to the peptide antibiotic nisin
Author(s) -
HansGeorg Sahl,
M Grossgarten,
William R. Widger,
William A. Cramer,
H. Brandis
Publication year - 1985
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.27.5.836
Subject(s) - nisin , peptide , lanthionine , lantibiotics , residue (chemistry) , lysine , biochemistry , amino acid , peptide sequence , size exclusion chromatography , chemistry , gel electrophoresis , sodium dodecyl sulfate , polyacrylamide gel electrophoresis , chromatography , biology , antimicrobial , organic chemistry , enzyme , gene
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.