Friulimicins: Novel Lipopeptide Antibiotics with Peptidoglycan Synthesis Inhibiting Activity from Actinoplanes friuliensis sp. nov: II. Isolation and Structural Characterization

Four novel lipopeptide antibiotics, friulimicins A, B, C, and D, were isolated from cultures of Actinoplanes friuliensis HAG 010964 after fermentation in different nutrient media. The new compounds were separated by ion-exchange chromatography from the acidic lipopeptides of the amphomycin type also...

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Published in:Journal of antibiotics 2000/08/25, Vol.53(8), pp.816-827
Main Authors: VÉRTESY, LÁSZLÓ, EHLERS, EBERHARD, KOGLER, HERBERT, KURZ, MICHAEL, MEIWES, JOHANNES, SEIBERT, GERHARD, VOGEL, MARTIN, HAMMANN, PETER
Format: Article
Language:English
Subjects:
Actinomycetales - metabolism
Actinoplanes friuliensis
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - isolation & purification
Antibiotics (antibacterial agents, antifungal agents)
Antibiotics, microbial producers, chemotherapic agents, antiseptics, disinfecting agents
Applied microbiology
Biological and medical sciences
friulimicins
Fundamental and applied biological sciences. Psychology
lipopeptide antibiotics
Magnetic Resonance Spectroscopy
Microbiology
Molecular Structure
Peptides
Peptidoglycan - biosynthesis
Peptidoglycan - drug effects
peptidoglycans
Protein Synthesis Inhibitors - chemistry
Protein Synthesis Inhibitors - isolation & purification
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Summary:Four novel lipopeptide antibiotics, friulimicins A, B, C, and D, were isolated from cultures of Actinoplanes friuliensis HAG 010964 after fermentation in different nutrient media. The new compounds were separated by ion-exchange chromatography from the acidic lipopeptides of the amphomycin type also present in the culture fluid, compounds A-1437 A, B, E, and G. The principal constituent friulimicin B, C59H94N14O19, was structurally characterized by mass spectrometric investigations of its hydrolysis and partial degradation products and by sequencing of the cyclic acyl peptide. The NMR data of friulimycin B and the amphomycin constituent A-1437 B were completely assigned by a variety of 2-D experiments, and confirmed the structures determined by mass spectrometry. All 8 lipopeptides possess an identical peptide macrocycle as their central element, linked via a diaminobutyric acid N-terminal either to an acylated asparagine residue or, in the case of the amphomycin series, to an acylated aspartic acid residue. The structures of the amphomycins have now been revised to take account of the peptide framework described herein and the determined cis-configuration of the exocyclic double bond. As a consequence of their higher isoelectric points, the new compounds friulimicin A, B, C, and D have different properties than the amphomycins.
ISSN:0021-8820
1881-1469
DOI:10.7164/antibiotics.53.816