STRUCTURAL ELUCIDATION OF AIBELLIN, A NEW PEPTIDE ANTIBIOTIC WITH EFFICIENCY ENHANCING ACTIVITY ON RUMEN FERMENTATION

Citation
S. Kumazawa et al., STRUCTURAL ELUCIDATION OF AIBELLIN, A NEW PEPTIDE ANTIBIOTIC WITH EFFICIENCY ENHANCING ACTIVITY ON RUMEN FERMENTATION, Journal of antibiotics, 47(10), 1994, pp. 1136-1144
Citations number
32
Categorie Soggetti
Pharmacology & Pharmacy",Immunology
Journal title
ISSN journal
00218820
Volume
47
Issue
10
Year of publication
1994
Pages
1136 - 1144
Database
ISI
SICI code
0021-8820(1994)47:10<1136:SEOAAN>2.0.ZU;2-P
Abstract
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 stru cture was elucidated from spectrometric analysis and chemical degradat ion. Aibellin is a 20-residue peptaibol, and it has a unique structura l feature in the novel C-terminal amino alcohol. Moreover, aibellin is the first peptaibol that possesses two acidic amino acids in the C-te rminal region and a Phe residue in the middle of the sequence.