Framycetin
Based on 1 publication(s) in Google Scholar
Framycetin (Neomycin B), an aminoglycoside antibiotic, is a potent RNase P cleavage activity inhibitor with a Ki of 35 μM. Framycetin competes for specific divalent metal ion binding sites in RNase P RNA. Framycetin inhibits hammerhead ribozyme with a Ki of 13.5 μM. Framycetin, a 5″-azido neomycin B precursor, binds the Drosha site in miR-525 and is used for hepatic encephalopathy and enteropathogenic E. coli infections.
The product specifications provided below refer solely to the active content of Framycetin.
For research use only. We do not sell to patients.
- CAS No.: 119-04-0
- Formula: C23H46N6O13
- Molecular Weight:614.64
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Storage:
Solution, -20°C, 2 years
Publications Citing Use of MedChemExpress (MCE) Framycetin
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Biological Activity
Description
The product specifications provided below refer solely to the active content of Framycetin.
IC50 & Target
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Aminoglycoside |
Cellular Effect
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Cell Line
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Type | Value | Description | References |
|---|---|---|---|---|
| 3LL cell line | IC50 |
>1 mM
Compound: Neomycin
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Cytotoxicity against mouse LLC cells assessed as reduction in cell viability
Cytotoxicity against mouse LLC cells assessed as reduction in cell viability
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[PMID: 36331380] |
| MDA-MB-231 | IC50 |
139 nM
Compound: NEO
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Binding affinity to rRNA-A site in human MDA-MB-231 cells assessed as inhibition of protein translation
Binding affinity to rRNA-A site in human MDA-MB-231 cells assessed as inhibition of protein translation
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[PMID: 30530174] |
In Vitro
The inhibition of RNase P RNA cleavage by Framycetin (Neomycin B; Fradiomycin B) is sensitive to pH and an increase in pH suppresses the inhibition in other systems[1].
Framycetin targets the bacterial and human ribosome and affect translation. 5″-azido neomycin B and Framycetin selectively inhibit production of the mature miRNA, boosts a downstream protein, and inhibits invasion in HCC cell line[2].
Framycetin binds to a structural rather than a sequence motif of the RNA. Its primary cognate target is the decoding site of the 16S rRNA, but it also binds to the Rev-responsive element in HIV-1, group I introns, and the hammerhead ribozyme, and thus inhibits their biological function[3].
Framycetin induces misreading of the genetic code during translation and inhibits several ribozymes. The ribosomal target site is the 16 S rRNA 1400 to 1500 region[4].
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
Chemical Information
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CAS No. 119-04-0
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Appearance Liquid
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Molecular Weight 614.64
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Formula C23H46N6O13
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Color Colorless to light yellow
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SMILES
N[C@@H](C[C@H]1N)[C@@]([C@@H]([C@H]1O)O[C@@](O[C@H](CO)[C@H]2O[C@@]([C@@H]([C@@H](O)[C@@H]3O)N)([H])O[C@H]3CN)([H])[C@@H]2O)([H])O[C@H]([C@@H]([C@@H](O)[C@@H]4O)N)O[C@@H]4CN
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Synonyms
Neomycin B; Fradiomycin B
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Shipping
Room temperature in continental US; may vary elsewhere.
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Storage
Solution, -20°C, 2 years
Publications (1)
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Journal Impact Factor
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Most Recent
Purity & Documentation
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Data Sheet (293 KB)
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SDS (419 KB)
- English - EN (419 KB)
- Français - FR (419 KB)
- Deutsch - DE (419 KB)
- Norwegian - NO (419 KB)
- Español - ES (419 KB)
- Swedish - SV (419 KB)
- Italian - IT (419 KB)
- Korean - KR (419 KB)
- Portuguese - PT (419 KB)
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Handling Instructions (2659 KB)
References
[1]. N E Mikkelsen, et al. Inhibition of RNase P RNA Cleavage by Aminoglycosides. Proc Natl Acad Sci U S A. 1999 May 25;96(11):6155-60. [Content Brief]
[2]. Childs-Disney JL, et al. Small Molecule Targeting of a MicroRNA Associated with Hepatocellular Carcinoma. ACS Chem Biol. 2016 Feb 19;11(2):375-80. [Content Brief]
[3]. Stampfl S, et al. Monovalent ion dependence of neomycin B binding to an RNA aptamer characterized by spectroscopic methods. Chembiochem. 2007 Jul 9;8(10):1137-45. [Content Brief]
[4]. Hoch I, et al. Antibiotic inhibition of RNA catalysis: neomycin B binds to the catalytic core of the td group I intron displacing essential metal ions. J Mol Biol. 1998 Sep 25;282(3):557-69. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)