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Structures of trichovirins II, peptaibol antibiotics from the mold Trichoderma viride NRRL 5243
Author(s) -
Jaworski Andreas,
Kirschbaum Jochen,
Brückner Hans
Publication year - 1999
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/(sici)1099-1387(199908)5:8<341::aid-psc204>3.0.co;2-0
Subject(s) - chromatography , chloroform , sephadex , chemistry , electrospray ionization , column chromatography , tandem mass spectrometry , mass spectrometry , trichoderma viride , elution , high performance liquid chromatography , formic acid , silica gel , biochemistry , enzyme , food science
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.