| Identification | Back Directory | [Name]
Nosiheptide | [CAS]
56377-79-8 | [Synonyms]
101159
CS-2680
RP 9671
priMofax
Nosiheptide
Multhiomycin
Nosiheptide VETRANAL
Nosiheptide USP/EP/BP
Nosiheptide (Multhiomycin)
Nosiheptide premix(0.25%,0.5%,1%)
4-Thiazolecarboxamide, N-[1-(aminocarbonyl)ethenyl]-2-[(11S,14Z,21S,23S,29S)-14-ethylidene-9,10,11,12,13,14,19,20,21,22,23,24,26,33,35,36-hexadecahydro-3,23-dihydroxy-11-[(1R)-1-hydroxyethyl]-31-methyl-9,12,19,24,33,43-hexaoxo-30,32-imino-8,5:18,15:40,37-trinitrilo-21,36-([2,4]-endo-thiazolomethanim...
N-[1-(Aminocarbonyl)ethenyl]-2-[(11S,14Z,21S,23S,29S)-14-ethylidene-9,10,11,12,13,14,19,20,21,22,23,24,26,33,35,36-hexadecahydro-3,23-dihydroxy-11-[(1R)-1-hydroxyethyl]-31-methyl-9,12,19,24,33,43-hexaoxo-30,32-imino-8,5:18,15:40,37-trinitrilo-21,36-([2,4]-endo-thiazolomethanimino)-5H,15H,37H-pyrido[3,2-w][2,11,21,27,31,7,14,17]benzoxatetrathiatriazacyclohexatriacontin-2-yl]-4-thiazolecarboxamide | [EINECS(EC#)]
260-138-4 | [Molecular Formula]
C51H43N13O12S6 | [MDL Number]
MFCD00867479 | [MOL File]
56377-79-8.mol | [Molecular Weight]
1222.34 |
| Chemical Properties | Back Directory | [Melting point ]
310-320° (dec) | [alpha ]
D20 +38° (c = 1 in pyridine) | [density ]
1.534±0.06 g/cm3(Predicted) | [storage temp. ]
Sealed in dry,Store in freezer, under -20°C | [solubility ]
DMSO (Slightly), Methanol (Slightly) | [form ]
Solid | [pka]
1.42±0.60(Predicted) | [color ]
Light Yellow to Light Brown |
| Hazard Information | Back Directory | [Uses]
Nosiheptide is a bicyclic thiopeptide antibiotic produced by several species of actinomycetes, notably Streptomyces, first reported by Japanese researchers in 1970. Unlike other bicyclic thiopeptides such as thiostrepton, the second macrocyclic ring is linked by relatively fragile lactone and thiolactone bridges to the core cyclic peptide. Nosiheptide has broad spectrum antibacterial activity, and has recently demonstrated a prolonged post-antibiotic effect in both nosocomial and community-acquired MRSA compared with vancomycin. Despite its long history in animal health, nosiheptide has not been extensively studied and is regarded as a “lost antibiotic” largely escaping intensive investigation for human application. | [Uses]
Nosiheptide is an antibacterial item used in feedstock and feed additives for chickens. | [Biological Activity]
mic: ≤ 0.25 mg/l for methicillin-resistant s. aureus strains; ≤ 0.125 mg/l for enterococcus spp; 0.008 mg/l for bi strain of c. difficilenosiheptide is a thiopeptide antibiotic.thiopeptides are a family of antibiotics counting with more than one hundred different entities. although thiopeptides are mainly isolated from soil bacteria, new members have been isolated from marine samples. thiopeptides have been reported to have a wide range of biological properties, such as antiplasmodial, anticancer, immunosuppressive, etc. | [in vitro]
the mode of action of nosiheptide on bacterial protein synthesis was found to be closely similar to that of thiostrepton. both antibiotics could inhibit functions of elongation factors tu and g and could also significantly reduce the synthesis of guanosine penta- and tetraphosphates to stringent factor. in addition, the actinomycetes that produced nosiheptide were able to defend themselves against their products in similar fashion, which involved specific pentosemethylation of 23s ribosomal rna [1]. | [in vivo]
the rhdl–nosiheptide complex was intravenously administered to male wistar rats and the distribution of nosiheptide in the liver and plasma was monitored 30 min after injection. results showed that the hepatic distribution of the rhdl–nosiheptide complex accounted for most of the administered nosiheptide, and was seven times as much as that in plasma. these findings indicated that the rhdl–nosiheptide complex could targete nosiheptide to the liver [2]. | [storage]
Store at -20°C | [References]
[1] e. cundliffe and j. thompson. the mode of action of nosiheptide (multhiomycin) and the mechanism of resistance in the producing organism. j.gen.microbiol. 126(1), 185-192 (1981).
[2] feng m, cai q, shi x, huang h, zhou p, guo x. recombinant high-density lipoprotein complex as a targeting system of nosiheptide to liver cells. j drug target. 2008 jul;16(6):502-8. |
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