Structural elucidation of aibellin, a new peptide antibiotic with efficiency enhancing activity on rumen fermentation.
A new peptide antibiotic, aibellin, that had the efficiency enhancing activity on rumen fermentation, was isolated from the culture broth of the fungus, Verticimonosporium ellipticum D1528, and its primary structure was elucidated from spectrometric analysis and chemical degradation. Aibellin is a 20-residue peptaibol, and it has a unique structural feature in the novel C-terminal amino alcohol. Moreover, aibellin is the first peptaibol that possesses two acidic amino acids in the C-terminal region and a Phe residue in the middle of the sequence.
Kumazawa
S
S
Yokohama Research Center, Mitsubishi Chemical Corporation, Japan.
Kanda
M
M
Aoyama
H
H
Utagawa
M
M
Kondo
J
J
Sakamoto
S
S
Ohtani
H
H
Mikawa
T
T
Chiga
I
I
Hayase
T
T
D000595:Amino Acid Sequence; D000605:Amino Alcohols / Q000737:chemistry; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D005285:Fermentation; D005658:Fungi / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010455:Peptides; D011487:Protein Conformation; D012417:Rumen / Q000187:drug effects* / Q000378:metabolism; D017421:Sequence Analysis
D000605:Amino Alcohols; D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D010455:Peptides; C083352:aibellin