Paracelsin; characterization by NMR spectroscopy and circular dichroism, and hemolytic properties of a peptaibol antibiotic from the cellulolytically active mnoldTrichoderma reesei. Part B

Autor: Brückner, H., Graf, H., Bokel, M.
Zdroj: Experientia; November 1984, Vol. 40 Issue: 11 p1189-1197, 9p
Abstrakt: Paracelsin, a hemolytic and membrane active polypeptide antibiotic of the peptaibol class which is excreted by the moldTrichderma reesei, was obtained by a simplified and isolation procedure utilziing hydrophobic adsorber resin. Investigation by13C nuclear magnetic resonance spectroscopy and circular dichroism revealed considerable helical portions in solution, and the very recently accomplished sequence determination of paracelsin allows the discussion of the results with regard to the closely related analogues, alamethicin and suzukacillin. A selective cleavage of the peptide was achieved by careful treatment with various acids, and a buffer of pH 8.25 and of high ionic strength made possible the quantitative determination of the C-terminal phenylalaninol released by means of ion-exchange chromatography. The significance of the production of paracelsin and related mycotoxins of the peptaibol class, exhibiting various kinds of biological activity, is discussed with respect to the extensive effort being made towards biotechnological applications of species, strains and cellulolytically highly active mutants of the fungusTrichoderma.
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