| Thiostrepton[1] | |
|---|---|
 |
|
| Other names | Alaninamide, Bryamycin, Thiactin |
| Identifiers | |
| CAS number | [] |
| PubChem | |
| SMILES |
|
| Properties | |
| Molecular formula | C72H85N19O18S5 |
| Molar mass | 1664.83 g/mol |
| Appearance | White to off-white powder |
| Melting point |
246-256 °C |
| Solubility in water | Insoluble |
| Solubility in other solvents | Soluble in CHCl3, CH2Cl2, dioxane, pyridine, glacial acetic acid, DMF. Practically insoluble in the lower alcohols, nonpolar organic solvents, diluted aqueous acids or bases. May be dissolved by methanolic acid or base, but with decomposition.[2] |
| Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa) Infobox references |
|
Thiostrepton is a natural cyclic oligopeptide antibiotic, derived from several strains of strepromycetes, such as Streptomyces azureus and Streptomyces laurentii.
History
Thiostrepton was discovered by Donovick et al. who described its antibacterial properties in 1955.[3] Dorothy Crowfoot Hodgkin solved the structure of thiostrepton in 1970.[4]
A total synthesis of Thiostrepton was completed by K.C. Nicolaou, et al. in 1995.
Applications
Thiostrepton has been used in veterinary medicine in mastitis caused by gram-negative organisms and in dermatologic disorders. It is mostly used in complex ointments containing neomycin, nystatin, Thiostrepton and topical steroids. It is also active against gram-positive bacteria. It is notable that ointments for human usage contain neomycin, nystatin, and topical steroids, but no Thiostrepton.
Recently, Thiostrepton has been reported to exhibit activity against breast cancer cells through targeting the transcription factor forkhead box M1.[5]
Thiostrepton is used in molecular biology as a reagent for both positive and negative selection of genes involved in nucleotide metabolism.
References
- ^ Merck Index, 11th Edition, 9295.
- ^ Thiostrepton product page at Fermentek
- ^ Donovick R, Pagano JF, Stout HA, Weinstein MJ (1955). Antibiot Annu 3: 554–9.
- ^ Anderson B, Crowfoot Hodgkin D, Viswamitra MA (1970). "The Structure of Thiostrepton". Nature 225: 223–235. doi:.
- ^ Kwok JM, Myatt SS, Marson CM, Coombes RC, Constantinidou D, Lam EW (July 2008). "Thiostrepton selectively targets breast cancer cells through inhibition of forkhead box M1 expression". Mol. Cancer Ther. 7 (7): 2022–32. doi:. PMID 18645012.
This entry is from Wikipedia, the leading user-contributed encyclopedia. It may not have been reviewed by professional editors (see full disclaimer)
