Sequences of polypeptide antibiotics stilboflavins, natural peptaibol libraries of the mold Stilbella flavipes

✍ Scribed by Andreas Jaworski; Hans Brückner

• Book ID: 105360148
• Publisher: John Wiley and Sons
• Year: 2001
• Tongue: English
• Weight: 654 KB
• Volume: 7
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/psc.335

✦ Synopsis

Abstract

From the culture broths of the mold Stilbella flavipes CBS 146.81, a mixture of polypeptides could be isolated by adsorption on XAD polystyrene resin and purified by Sephadex LH‐20 chromatography. Using preparative thin‐layer chromatography (TLC) three groups of peptides, named stilboflavins (SF) A, B, and C could be separated. Each of the groups showed microheterogeneity when investigated by high‐performance liquid chromatography (HPLC). Employing on‐line HPLC‐electrospray ionization tandem mass spectrometry in the positive and negative ionization mode, together with gas chromatography‐selected ion monitoring mass spectrometry, enantioselective GC and quantitative amino acid analysis, the sequences of stilboflavins A and B could be determined. Exchange of Glu in stilboflavins A peptides (acidic) against Gln in stilboflavins B peptides (neutral) is the rational for different polarity of the peptide groups and their separatability by TLC. Since SF A and B are bioactive __N‐__acetylated 20‐residue peptides with a high proportion of α‐aminoisobutyric acid and __C‐__terminal bonded amino alcohols (either leucinol, isoleucinol or valinol) the peptides belong to the group of peptaibol antibiotics. Copyright © 2001 European Peptide Society and John Wiley & Sons, Ltd.