Structural characterization of lichenysin A components by fast atom bombardment tandem mass spectrometry.
The structural characterization of the cyclic lipoheptapeptide surfactant lichenysin A components, produced by Bacillus licheniformis strains via the non-ribosomal pathway on a corresponding peptide synthetase, was carried out using a tandem mass spectrometry (MS/MS) under fast atom bombardment (FAB) conditions. Based on the analysis of the collision-induced fragment-ion spectrum of the single charged molecular ions of both native and partially hydrolyzed forms of lipopeptide, a new general structure of lichenysin A components was elucidated. It varies from previously proposed structure by having in the peptide portion of lipopeptide the L-Gln-1 and L-Asp-5 residues instead of L-Glu-1 and L-Asn-5. The verified chemical structure of lichenysin A was found to be reflected in the structural organization of the corresponding lichenysin A synthetase, LchA, described recently.
D001407:Bacillus / Q000737:chemistry; D008074:Lipoproteins / Q000737:chemistry*; D015394:Molecular Structure; D010456:Peptides, Cyclic / Q000737:chemistry*; D016339:Spectrometry, Mass, Fast Atom Bombardment