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Identification
Name Framycetin
Accession Number DB00452 (APRD00618)
Type small molecule
Groups approved
Description

A component of neomycin that is produced by Streptomyces fradiae. On hydrolysis it yields neamine and neobiosamine B. (From Merck Index, 11th ed)
Structure Thumb
Download: MOL | SDF | SMILES | InChI
Display: 2D Structure | 3D Structure
Synonyms
Framycetinum [INN-Latin]
Neomycin B
Streptothricin B
Salts Not Available
Brand names
Name Company
Actilin
Actiline
Antibiotique
Dekamycin V
Enterfram
Fradiomycin B
Framygen
Nebramycin X
Negamicin
Neomycin A
Soframycin
Soframycin Ophthalmic
Soframycine
First Prev Next Last
Brand mixtures Not Available
Categories
  • Anti-Bacterial Agents
  • Antibiotics
  • Aminoglycosides
CAS number 119-04-0
Weight Average: 614.6437
Monoisotopic: 614.312285588
Chemical Formula C23H46N6O13
InChI Key InChIKey=PGBHMTALBVVCIT-VCIWKGPPSA-N
InChI
InChI=1S/C23H46N6O13/c24-2-7-13(32)15(34)10(28)21(37-7)40-18-6(27)1-5(26)12(31)20(18)42-23-17(36)19(9(4-30)39-23)41-22-11(29)16(35)14(33)8(3-25)38-22/h5-23,30-36H,1-4,24-29H2/t5-,6+,7-,8+,9-,10-,11-,12+,13-,14-,15-,16-,17-,18-,19-,20-,21-,22-,23+/m1/s1
Plain Text
IUPAC Name
(2R,3S,4R,5R,6R)-5-amino-2-(aminomethyl)-6-{[(1R,2R,3S,4R,6S)-4,6-diamino-2-{[(2S,3R,4S,5R)-4-{[(2R,3R,4R,5S,6S)-3-amino-6-(aminomethyl)-4,5-dihydroxyoxan-2-yl]oxy}-3-hydroxy-5-(hydroxymethyl)oxolan-2-yl]oxy}-3-hydroxycyclohexyl]oxy}oxane-3,4-diol
SMILES
NC[C@@H]1O[C@H](O[C@@H]2[C@@H](CO)O[C@@H](O[C@@H]3[C@@H](O)[C@H](N)C[C@H](N)[C@H]3O[C@H]3O[C@H](CN)[C@@H](O)[C@H](O)[C@H]3N)[C@@H]2O)[C@H](N)[C@@H](O)[C@@H]1O
Plain Text
Mass Spec Not Available
Taxonomy
Kingdom Organic
Classes
  • Aminoglycosides
Substructures
  • Aminoglycosides
  • Glycerol and Derivatives
  • Hydroxy Compounds
  • Pyrans
  • Acetals and Derivatives
  • Aliphatic and Aryl Amines
  • Ethers
  • Alcohols and Polyols
  • Amino Alcohols
  • Heterocyclic compounds
  • Carbohydrates
  • Furans
Pharmacology
Indication For the treatment of bacterial blepharitis, bacterial bonjunctivitis, corneal injuries, corneal ulcers and meibomianitis. For the prophylaxis of ocular infections following foreign body removal
Pharmacodynamics Framycetin is used for the treatment of bacterial eye infections such as conjunctivitis. Framycetin is an antibiotic. It is not active against fungi, viruses and most kinds of anaerobic bacteria. Framycetin works by binding to the bacterial 30S ribosomal subunit, causing misreading of t-RNA, leaving the bacterium unable to synthesize proteins vital to its growth. Framycetin is useful primarily in infections involving aerobic bacteria bacteria.
Mechanism of action Framycetin binds to specific 30S-subunit proteins and 16S rRNA, four nucleotides of 16S rRNA and a single amino acid of protein S12. This interferes with decoding site in the vicinity of nucleotide 1400 in 16S rRNA of 30S subunit. This region interacts with the wobble base in the anticodon of tRNA. This leads to interference with the initiation complex, misreading of mRNA so incorrect amino acids are inserted into the polypeptide leading to nonfunctional or toxic peptides and the breakup of polysomes into nonfunctional monosomes.
Absorption Not Available
Volume of distribution Not Available
Protein binding Not Available
Metabolism
Not Available
Route of elimination Not Available
Half life Not Available
Clearance Not Available
Toxicity Not Available
Affected organisms
  • Enteric bacteria and other eubacteria
Pathways Not Available
Pharmacoeconomics
Manufacturers Not Available
Packagers
Dosage forms
Form Route Strength
Dressing Topical
Ointment Ophthalmic
Solution / drops Ophthalmic
Prices
Unit description Cost Unit
Neomycin Sulfate 500 mg tablet 1.39 USD tablet
Neomycin 500 mg tablet 1.25 USD tablet
Neomycin sulfate powder 0.84 USD g
DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.
Patents Not Available
Properties
State solid
Experimental Properties
Property Value Source
logP -7.8 Not Available
Predicted Properties
Property Value Source
water solubility 6.47e+01 g/l ALOGPS
logP -2.8 ALOGPS
logP -8.4 ChemAxon
logS -0.98 ALOGPS
pKa (strongest acidic) 12.29 ChemAxon
pKa (strongest basic) 9.97 ChemAxon
physiological charge 6 ChemAxon
hydrogen acceptor count 19 ChemAxon
hydrogen donor count 13 ChemAxon
polar surface area 353.11 ChemAxon
rotatable bond count 9 ChemAxon
refractivity 135.9 ChemAxon
polarizability 60.87 ChemAxon
References
Synthesis Reference Not Available
General Reference Not Available
External Links
Resource Link
PubChem Compound 8378 Link_out
PubChem Substance 46508892 Link_out
ChemSpider 8075 Link_out
BindingDB 19 Link_out
ChEBI 7508 Link_out
ChEMBL 7508 Link_out
Therapeutic Targets Database DNC001005 Link_out
PharmGKB PA164743181 Link_out
Drug Product Database 2224887 Link_out
Wikipedia http://en.wikipedia.org/wiki/Framycetin Link_out
ATC Codes
  • D09AA01
  • R01AX08
  • S01AA07
AHFS Codes
  • 84:04.04
  • 52:04.04
PDB Entries Not Available
FDA label Not Available
MSDS Not Available
Interactions
Drug Interactions Not Available
Food Interactions Not Available
Targets

1. 16S rRNA

Pharmacological action: yes
Actions: inhibitor

In prokaryotes, the 16S rRNA is essential for recognizing the 5' end of mRNA and hence positioning it correctly on the ribosome. The 16S rRNA has a characteristic secondary structure in which half of the nucleotides are base-paired. The 16S rRNA sequence has been highly conserved and is often used for evolutionary and species comparative analysis.

Gene Sequence: FASTA

References:
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed
  3. Chao PW, Chow CS: Monitoring aminoglycoside-induced conformational changes in 16S rRNA through acrylamide quenching. Bioorg Med Chem. 2007 Jun 1;15(11):3825-31. Epub 2007 Mar 13. Pubmed

2. 30S ribosomal protein S12

Pharmacological action: yes
Actions: inhibitor

Cryo-EM studies suggest that S12 contacts the EF-Tu bound tRNA in the A-site during codon-recognition. This contact is most likely broken as the aminoacyl-tRNA moves into the peptidyl transferase center in the 50S subunit

Organism class: bacterial
UniProt ID: P0A7S3 Link_out
Gene: rpsL
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed
  3. Famulok M, Huttenhofer A: In vitro selection analysis of neomycin binding RNAs with a mutagenized pool of variants of the 16S rRNA decoding region. Biochemistry. 1996 Apr 9;35(14):4265-70. Pubmed

3. C-X-C chemokine receptor type 4

Pharmacological action: unknown
Actions: antagonist

Receptor for the C-X-C chemokine CXCL12/SDF-1. Transduces a signal by increasing the intracellular calcium ions level. Involved in haematopoiesis and in cardiac ventricular septum formation. Plays also an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodelling processes in endothelial cells. Could be involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival. Acts as a coreceptor (CD4 being the primary receptor) for HIV-1 X4 isolates and as a primary receptor for some HIV-2 isolates. Promotes Env-mediated fusion of the virus

Organism class: human
UniProt ID: P61073 Link_out
Gene: CXCR4 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Litovchick A, Lapidot A, Eisenstein M, Kalinkovich A, Borkow G: Neomycin B-arginine conjugate, a novel HIV-1 Tat antagonist: synthesis and anti-HIV activities. Biochemistry. 2001 Dec 25;40(51):15612-23. Pubmed
  2. Borkow G, Vijayabaskar V, Lara HH, Kalinkovich A, Lapidot A: Structure-activity relationship of neomycin, paromomycin, and neamine-arginine conjugates, targeting HIV-1 gp120-CXCR4 binding step. Antiviral Res. 2003 Nov;60(3):181-92. Pubmed
Comments
Drug created on June 13, 2005 07:24 / Updated on February 08, 2013 16:19