Structure of fuscopeptins, phytotoxic metabolites of Pseudomonas fuscovaginae

• Published in: FEBS letters Vol. 381; no. 3; pp. 213 - 216
• Main Authors: Ballio, A., Bossa, F., Camoni, L., Di Giorgio, D., Flamand, M.-C., Maraite, H., Nitti, G., Pucci, P., Scaloni, A.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 04.03.1996
• Subjects: Amino Acid Sequence; aThr, allothreonine; Bacterial Proteins - pharmacology; Bacterial Toxins - chemistry; Bacterial Toxins - isolation & purification; Bacterial Toxins - pharmacology; Dab, 2,4-diaminobutyric acid; Dhb, 2,3-dehydro-2-aminobutyric acid; FAB-MS, fast atom bombardment mass spectrometry; FP, fuscopeptin; Fungi - drug effects; Fuscopeptins; GC-MS, gas chromatography mass spectrometry; Lipodepsipeptides; Magnetic Resonance Spectroscopy; Microbial Sensitivity Tests; Molecular Sequence Data; Peptides, Cyclic - chemistry; Peptides, Cyclic - isolation & purification; Peptides, Cyclic - pharmacology; Phytotoxins; Plant Diseases - microbiology; Pseudomonas - metabolism; Pseudomonas fuscovaginae; SP, syringopeptin; Spectrometry, Mass, Fast Atom Bombardment; SR, syringomycin; Structure-Activity Relationship; TBDMS, t-butyldimethylsilyl; TFA, trifluoroacetic acid; Fuscopeptins; Phytotoxins; Dab, 2,4-diaminobutyric acid; GC-MS, gas chromatography mass spectrometry; FAB-MS, fast atom bombardment mass spectrometry; Pseudomonas fuscovaginae; FP, fuscopeptin; aThr, allothreonine; Lipodepsipeptides; Dhb, 2,3-dehydro-2-aminobutyric acid; SR, syringomycin; TBDMS, t-butyldimethylsilyl; SP, syringopeptin; TFA, trifluoroacetic acid
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(96)00043-9

The structure of the fuscopeptins, bioactive lipodepsipeptides produced in culture by the gramineae pathogen Pseudomonas fuscovaginae, has been determined. The combined use of FAB mass spectrometry, NMR spectroscopy and chemical and enzymatic procedures allowed one to define a peptide moiety corresponding to ZDhb-DPro-LLeu-DAla-DAla-DAla-DAlaDVal-Gly-DAla-DVal-DAla-DVal-ZDhb-DaThr-LAla-LDabDDab-LPhe with the terminal carboxyl group closing a macrocyclic ring on the hydroxyl group of the allothreonine residue. The N-terminus is in turn acylated by 3-hydroxyoctanoate in fuscopeptin A and 3-hydroxydecanoate in fuscopeptin B. Some preliminary data on the biological activity of fuscopeptins are also reported.