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

From the culture broths of the mold Stilbella flavipes CBS 146.81, a mixtur e 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). Employi ng on-line HPLC-electrospray ionization tandem mass spectrometry in the pos itive and negative ionization mode, together with gas chromatography-select ed ion monitoring mass spectrometry, enantioselective GC and quantitative a mino acid analysis, the sequences of stilboflavins A and B could be determi ned. Exchange of Glu in stilboflavins A peptides (acidic) against Gln in st ilboflavins A peptides (neutral) is the rational for different polarity of the peptide groups and their separatability by TLC. Since SF A and B are bi oactive N-acetylated 20-residue peptides with a high proportion of alpha -a minoisobutyric acid and C-terminal bonded amino alcohols (either leucinol, isoleucinol or valinol) the peptides belong to the group of peptaibol antib iotics. Copyright (C) 2001 European Peptide Society and John Wiley & Sons, Ltd.