Framycetin  (Synonyms: Neomycin B; Fradiomycin B)

Framycetin (Neomycin B), an aminoglycoside antibiotic, is a potent RNase P cleavage activity inhibitor with a K_i of 35 μM. Framycetin competes for specific divalent metal ion binding sites in RNase P RNA. Framycetin inhibits hammerhead ribozyme with a K_i 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^[1][2].

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.

614.64

C₂₃H₄₆N₆O₁₃

119-04-0

Liquid

Colorless to light yellow

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

Room temperature in continental US; may vary elsewhere.

Solution, -20°C, 2 years

• [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]