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

✍ Scribed by Andreas Jaworski; Jochen Kirschbaum; Hans Brückner

• Book ID: 101284134
• Publisher: John Wiley and Sons
• Year: 1999
• Tongue: English
• Weight: 139 KB
• Volume: 5
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/(sici)1099-1387(199908)5:8<341::aid-psc204>3.0.co;2-0

✦ Synopsis

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 h-aminoisobutyric acid (Aib) residues and the bactericidal and hemolytic activity, the peptides belong to the family of peptaibol antibiotics.