Work

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

Year: 1985

Type: article

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.

Source: Antimicrobial Agents and Chemotherapy

DOI: 10.1128/aac.27.5.836

Authors: H G Sahl, M Grossgarten, W R Widger, W A Cramer, H Brandis

Language: English

Topic: Antimicrobial Peptides and Activities

Subfield: Microbiology

Field: Immunology and Microbiology

Domain: Life Sciences

Open Access status: green

Funders: Deutsche Forschungsgemeinschaft, National Institutes of Health, National Institute of General Medical Sciences

Award: Receptor-mediated Colicin Import

OpenAlex ID: W2035610941

FWCI: 2.99

Cites: 15

Cited by: 59

Related to: 10