The tetracyclic lantibiotic actagardine. 1H-NMR and 13C-NMR assignments and revised primary structure.
The primary structure of the peptide lantibiotic actagardine was determined in (2H3)acetonitrile/H2O by homonuclear two- and three-dimensional NMR spectroscopy as well as 2D 1H(13C) correlation spectra at natural abundance. Actagardine was found to be a tetracyclic 19-residue peptide containing one lanthionine and three overlapping beta-methyllanthionine bridges. Sequential resonance assignment and location of the four thioether rings was accomplished by 2D NOESY, 3D NOESY-TOCSY and gradient-enhanced 1H(13C)-HMBC spectra. The C-terminal thioether bridge was shown to be oxidized to a sulfoxide. The NMR data were additionally confirmed by mass spectrometry and Edman degradation after chemical modification, which allowed sequencing of lanthionine and beta-methyllanthionine residues. Our studies clearly show, that the structure of actagardine as previously published by Kettenring et al. (1990) J. Antibiot. 43, 1082-1088 is not correct.[1]References
- The tetracyclic lantibiotic actagardine. 1H-NMR and 13C-NMR assignments and revised primary structure. Zimmermann, N., Metzger, J.W., Jung, G. Eur. J. Biochem. (1995) [Pubmed]
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