Thiostrepton

Catalog No.S4354 Batch:S435401

Technical Data

Formula	C₇₂H₈₅N₁₉O₁₈S₅
Molecular Weight	1664.89	CAS No.	1393-48-2
Solubility (25°C)*	In vitro


* <1 mg/ml means slightly soluble or insoluble. * Please note that Selleck tests the solubility of all compounds in-house, and the actual solubility may differ slightly from published values. This is normal and is due to slight batch-to-batch variations. * Room temperature shipping (Stability testing shows this product can be shipped without any cooling measures.)

Biological Activity

Description	Thiostrepton (Alaninamide, Bryamycin, Thiactin) is a natural cyclic oligopeptide antibiotic, derived from several strains of strepromycetes.
In vitro	Thiostrepton inhibits growth of the parasite in the micromolar range which is 10-fold below concentrations with observable effects on total protein synthesis. Thiostrepton results in disappearance of organellar-encoded RNA transcripts within 6 hours of treatment while transcripts of a nuclear-encoded mRNA remain constant for at least 8 hous of treatment. Thiostrepton directly interacts with two nucleotides in the GTPase domain of Escherichia coli. ^[1] Thiostrepton directly interacts the region around position 1067 in domain II of 23S rRNA inhibits GTP hydrolysis by elongation factor G (EF-G) on the ribosome at the conditions of multiple turnover. Thiostrepton interferes with EF-G footprints in the alpha-sarcin stem loop (A2660, A2662) located in domain VI of 23S rRNA. ^[2] Thiostrepton interacts with a 58-nucleotide domain of large subunit ribosomal RNA, and binds to the ribosome cooperatively with Ribosomal protein L11. Thiostrepton and RNA recognition cooperativity can be attributed to N- and C-terminal domains of L11, respectively. ^[3] Thiostrepton binds primarily to 23 S rRNA, thus probably inhibits peptide elongation by impeding a conformational change within protein L11 that is important for the function of the ribosomal GTPase centre. ^[4] Thiostrepton (10 μM) treatment reduces FOXM1 expression in a time- and dose-dependent manner, independent of de novo protein synthesis and predominantly at transcriptional and gene promoter levels. Thiostrepton (10 μM) induces cell cycle arrest at G(1) and S phases and cell death, concomitant with FOXM1 repression in breast cancer cells. Thiostrepton (10 μM) also shows efficacy in repressing breast cancer cell migration, metastasis, and transformation, which are all downstream functional attributes of FOXM1. ^[5]

Description

Thiostrepton (Alaninamide, Bryamycin, Thiactin) is a natural cyclic oligopeptide antibiotic, derived from several strains of strepromycetes.

In vitro

Thiostrepton inhibits growth of the parasite in the micromolar range which is 10-fold below concentrations with observable effects on total protein synthesis. Thiostrepton results in disappearance of organellar-encoded RNA transcripts within 6 hours of treatment while transcripts of a nuclear-encoded mRNA remain constant for at least 8 hous of treatment. Thiostrepton directly interacts with two nucleotides in the GTPase domain of Escherichia coli. ^[1] Thiostrepton directly interacts the region around position 1067 in domain II of 23S rRNA inhibits GTP hydrolysis by elongation factor G (EF-G) on the ribosome at the conditions of multiple turnover. Thiostrepton interferes with EF-G footprints in the alpha-sarcin stem loop (A2660, A2662) located in domain VI of 23S rRNA. ^[2] Thiostrepton interacts with a 58-nucleotide domain of large subunit ribosomal RNA, and binds to the ribosome cooperatively with Ribosomal protein L11. Thiostrepton and RNA recognition cooperativity can be attributed to N- and C-terminal domains of L11, respectively. ^[3] Thiostrepton binds primarily to 23 S rRNA, thus probably inhibits peptide elongation by impeding a conformational change within protein L11 that is important for the function of the ribosomal GTPase centre. ^[4] Thiostrepton (10 μM) treatment reduces FOXM1 expression in a time- and dose-dependent manner, independent of de novo protein synthesis and predominantly at transcriptional and gene promoter levels. Thiostrepton (10 μM) induces cell cycle arrest at G(1) and S phases and cell death, concomitant with FOXM1 repression in breast cancer cells. Thiostrepton (10 μM) also shows efficacy in repressing breast cancer cell migration, metastasis, and transformation, which are all downstream functional attributes of FOXM1. ^[5]

Protocol (from reference)

References

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Selleck's Thiostrepton has been cited by 3 publications

Selective BD2 Inhibitor Exerts Anti-Fibrotic Effects via BRD4/FoxM1/Plk1 Axis in Orbital Fibroblasts From Patients With Thyroid Eye Disease [ Invest Ophthalmol Vis Sci, 2023, 64(7):9]	PubMed: 37272763
Targetable vulnerability of deregulated FOXM1/PLK1 signaling axis in diffuse large B cell lymphoma [ Am J Cancer Res, 2022, 12(10:4666-4679)]	PubMed: 36381323
Thiostrepton reactivates latent HIV-1 through p-TEFb and NF-κB pathway mediated by heat shock response. [ Antimicrob Agents Chemother, 2020, 10.1128/AAC.02328-19]	PubMed: 32094131

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SHIPPING AND STORAGE
Selleck products are transported at room temperature. If you receive the product at room temperature, please rest assured, the Selleck Quality Inspection Department has conducted experiments to verify that the normal temperature placement of one month will not affect the biological activity of powder products. After collecting, please store the product according to the requirements described in the datasheet. Most Selleck products are stable under the recommended conditions.

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