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Thiopeptin, a New Feed Additive Antibiotic: Microbiological and Chemical Studies

The thiopeptins are a new group of sulfur-containing peptide antibiotics produced by Streptomyces tateyamensis. The antibiotic consists of a major component (designated as thiopeptin B) and four minor ones (thiopeptins A1 to A4). These components were isolated by solvent extraction from mycelium followed by chromatography on silica gel with various ratios of chloroform and methanol as elution solvents. Acid hydrolysis of each of the thiopeptin components yielded 1 mole of valine, 1 of threonine, 1 of cysteine, and 2 of alanine as amino acids. Each component of the thiopeptin A group has chemical and biological properties closely similar to those of thiopeptin B, but detailed characterization has established that thiopeptins A1, A3, and A4 are new antibiotics. We could not obtain accurate data for determination of the uniqueness of A2 because of insufficient sample. Thiopeptin has strong antibacterial activity against gram-positive bacteria and Mycoplasma, and exhibits no cross-resistance to major human-use antibiotics.