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Structures of trichovirins II, peptaibol antibiotics from the moldTrichoderma viride NRRL 5243

1999; Wiley; Volume: 5; Issue: 8 Linguagem: Inglês

10.1002/(sici)1099-1387(199908)5

1099-1387

Andreas Jaworski, Jochen Kirschbaum, Hans Brückner,

Microbial Natural Products and Biosynthesis

From the culture broth of the mold Trichoderma viride NRRL 5243 a mixture of polypeptides, named trichovirins (TV), could be isolated and purified by chromatography on XAD-2 adsorber resin and Sephadex LH-20 gel. Chromatography on silica gel using chloroform/methanol 8:2 as eluent provided a mixture of peptides named TV I. Subsequent elution with chloroform/methanol 1:1 yielded a second group of peptides named TV II. That group could be separated into individual components by repetitive HPLC on an octadecylsilyl and a fluorocarbon stationary phase. The sequences of 12 peptides of TV II could be determined by electrospray ionization tandem mass spectrometry of isolated peptides and gas chromatography-mass spectrometry of methanolysates. The N-termini of the 18-mer peptides are acetylated and the C-termini consist of leucinol. Owing to the presence of α-aminoisobutyric acid (Aib) residues and the bactericidal and hemolytic activity, the peptides belong to the family of peptaibol antibiotics. Copyright © 1999 European Peptide Society and John Wiley & Sons, Ltd.