Total structure of the peptide antibiotic components of thiopeptin by 1H and 13C NMR spectroscopy

✍ Scribed by Otto D. Hensens; Georg Albers-Schönberg

• Book ID: 104246044
• Publisher: Elsevier Science
• Year: 1978
• Tongue: French
• Weight: 268 KB
• Volume: 19
• Category: Article
• ISSN: 0040-4039
• DOI: 10.1016/s0040-4039(01)95020-8

✦ Synopsis

Thiopeptin, produced by Streptomyces tateyamensis and belonging to a group of highly modified sulfur-containing peptide antibiotics is a valuable growth promotant in swine and chickens' and was shown to be effective as a lactic-acidosis preventive in sheep and cattle'. The antibiotic complex was characterized by Miyairi et al3 and shown to consist of a major component B and four minor components Al, AZ, A3 and A4. No structures for any of the components have been reported although acid hydrolysis experiments 4 , primarily on thiopeptin B, have demonstrated a close relationship to thiostrepton, the structure of which was largely determined by X-ray crystallog-raphy5 and its side-chain by 13C NMR spectroscopy6.

We wish to report here on the structure determination of the various thiopeptin components primarily by lH and 13C NMR techniques.