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

HansGeorg Sahl | Zendy; M Grossgarten | Zendy; William R. Widger | Zendy; William A. Cramer | Zendy; H. Brandis | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Structural 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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research