SKU: N042  / 
    CAS Number: 56377-79-8

    Nosiheptide

    ฿3,777.64 - ฿13,221.96

    Nosiheptide is a broad-spectrum bicyclic thiopeptide antibiotic produced by several species of actinomycetes (ie Streptomyces) and was first reported by Japanese researchers in 1970. It has a prolonged post-antibiotic effect in both nosocomial and community-acquired MRSA. Despite its long history in animal health research, Nosiheptide has not been extensively studied.

    Nosiheptide is soluble in ethanol, methanol, DMF and DMSO. 

    Mechanism of Action Nosiheptide impacts bacterial protein synthesis in a similar fashion to that of thiostrepton. However unlike thiostrepton, the second macrocyclic ring is linked by relatively fragile lactone and thiolactone bridges to the core cyclic peptide. Nosiheptide inhibits the elongation factors Tu and G and greatly reduce the synthesis of guanosine penta- and tetraphosphates. This involves pentose-methylation of 23S ribosomal RNA. 

    Research suggests that the Nosiheptides biosynthetic machinery can lead to engineering novel thiopeptides for drug discovery (Yu et al, 2009).
    Spectrum Broad-spectrum, effective for Gram-negative and Gram-positive bacteria. It is also effective against MRSA.
    Molecular Formula C51H43N13O12S6
    References

    Cundiffe E an Thompson J (1981)  The mode of action of Nisiheptide (multhiomycin) and the mechanism of resistance in the producing organism. J. Gen. Microbiol. 126(1):185-192  PMID 7038038

    Endo T and Yonehara HJ  (1978)  Identity of multhiomycin with Nosiheptide. 31:623

    Haste NM et al. (2012)  Activity of the thiopeptide antibiotic, Nosiheptide, against contemporary strains of methicillin-resistant Staphylococcus aureus. Antibiot. 65:593

    Pestka S and Bodley J (1975)  Thiostrepton group of antibiotics. In: Antibiotics. III. eds. Corcoran JW. & Harn FE., Springer-Verlag, New York. pp 551-573

    Tanaka T et al (1970)  A new antibiotic, multhiomycin. J. Antibiot.  23:231

    Yu Y et al (2009)  Noiheptide biosynthesis featuring a unique indole side ring formation on the characteristic thiopeptide framework. ACS Chem. Biol 4(10):855-864