Thiostrepton

Thiostrepton is a natural cyclic oligopeptide antibiotic of the thiopeptide class, derived from several strains of streptomycetes, such as Streptomyces azureus and Streptomyces laurentii. Thiostrepton is a natural product of the ribosomally synthesized and post-translationally modified peptide (RiPP) class. Thiostrepton is a natural cyclic oligopeptide antibiotic of the thiopeptide class, derived from several strains of streptomycetes, such as Streptomyces azureus and Streptomyces laurentii. Thiostrepton is a natural product of the ribosomally synthesized and post-translationally modified peptide (RiPP) class. Thiostrepton was discovered by Donovick et al. who described its antibacterial properties in 1955. Dorothy Crowfoot Hodgkin solved the structure of thiostrepton in 1970.Early in 1978, Bycroft and Gowlandproposed the biosynthesis of thiostrepton, which was still unclear until 2009. Several studies of thiopeptide biosynthesis have been contemporarily published in 2009 and two of them (Liao et al. and Kelly et al.) included the similar biosynthesis of thiostrepton: it's ribosomally synthesized from thiostrepton biosynthetic genes (tsr genes) and posttranslational modification is needed. A total synthesis of thiostrepton was completed by K.C. Nicolaou, et al. in 2004. 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. Thiostrepton was reported (in 2008) to exhibit activity against breast cancer cells through targeting the transcription factor forkhead box M1 (FOXM1), also in 2011.It has also been shown to circumvent acquired cisplatin resistance in breast cancer cells under in invitro conditions.