Arylomycins A and B, new biaryl-bridged lipopeptide antibiotics produced by Streptomyces sp. Tü 6075. II. Structure elucidation

J Antibiot (Tokyo). 2002 Jun;55(6):571-7. doi: 10.7164/antibiotics.55.571.


The structures of new lipopeptide antibiotics, arylomycins A and B, were elucidated by a combination of ESI-FTICR-mass spectrometry, NMR spectroscopy, Edman sequencing, and fatty acid and chiral amino acid analyses. The colourless arylomycins A share the peptide sequence of D-N-methylseryl2(D-MeSer2)-D-alanyl3-glycyl4-N-methyl- 4-hydroxyphenylglycyl5(MeHpg5)-L-alanyl6-tyrosine7 cyclised by a [3,3]biaryl bond between MeHpg5 and Tyr7. The yellow arylomycins B differ from arylomycins A by nitro substitution of Tyr7. The N-termini of arylomycins A and B are acylated with saturated C11-C15 fatty acids (fa1) comprising n, iso, and anteiso isomers. Arylomycins A and B represent the first examples of biaryl-bridged lipopeptides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Anti-Bacterial Agents / chemistry*
  • Anti-Bacterial Agents / isolation & purification
  • Fatty Acids / analysis
  • Gas Chromatography-Mass Spectrometry
  • Magnetic Resonance Spectroscopy
  • Peptides, Cyclic / chemistry*
  • Peptides, Cyclic / isolation & purification
  • Sequence Analysis, Protein
  • Streptomyces / chemistry*


  • Amino Acids
  • Anti-Bacterial Agents
  • Fatty Acids
  • Peptides, Cyclic