Taribavirin

This drug entry is a stub and has not been fully annotated. It is scheduled to be annotated soon.

Identification

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Name
Taribavirin
Accession Number
DB06408
Type
Small Molecule
Groups
Investigational
Description
Not Available
Structure
Thumb
Synonyms
  • Ribavirin amidine
  • Taribavirin
  • Viramidine
External IDs
ICN 3142
Product Ingredients
IngredientUNIICASInChI Key
Taribavirin hydrochlorideD22JZE246P40372-00-7PIGYMBULXKLTCJ-UHSSARMYSA-N
Categories
UNII
R3B1994K2E
CAS number
119567-79-2
Weight
Average: 243.223
Monoisotopic: 243.096753919
Chemical Formula
C8H13N5O4
InChI Key
NHKZSTHOYNWEEZ-AFCXAGJDSA-N
InChI
InChI=1S/C8H13N5O4/c9-6(10)7-11-2-13(12-7)8-5(16)4(15)3(1-14)17-8/h2-5,8,14-16H,1H2,(H3,9,10)/t3-,4-,5-,8-/m1/s1
IUPAC Name
1-[(2R,3R,4S,5R)-3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]-1H-1,2,4-triazole-3-carboximidamide
SMILES
NC(=N)C1=NN(C=N1)[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O

Pharmacology

Indication

Investigated for use/treatment in hepatitis (viral, C).

Pharmacodynamics
Not Available
Mechanism of action

The prodrug taribavirin (1-b-D-ribofuranosyl-1H-1, 2, 4-triazole-3-carboxamidine) is a synthetic nucleoside (guanosine) analog under development for the treatment of patients with chronic hepatitis C. Taribavirin is metabolized by the liver and converted into its active metabolite, ribavirin. This pathway reduces exposure to red blood cells (RBCs) and increases exposure to the liver, the site of HCV replication. [Valeant Website] Ribavirin is readily phosphorylated intracellularly by adenosine kinase to ribavirin mono-, di-, and triphosphate metabolites. Ribavirin triphosphate (RTP) is a potent competitive inhibitor of inosine monophosphate (IMP) dehydrogenase, viral RNA polymerase and messenger RNA (mRNA) guanylyltransferase (viral). Guanylyltranserase inhibition stops the capping of mRNA. These diverse effects result in a marked reduction of intracellular guanosine triphosphate (GTP) pools and inhibition of viral RNA and protein synthesis. Ribavirin is also incorporated into the viral genome causing lethal mutagenesis and a subsequent decrease in specific viral infectivity.

TargetActionsOrganism
URNA-directed RNA polymerase catalytic subunitNot AvailableInfluenza A virus (strain A/Beijing/11/1956 H1N1)
UCytosolic purine 5'-nucleotidaseNot AvailableHumans
UInosine-5'-monophosphate dehydrogenase 1Not AvailableHumans
UDNANot AvailableHumans
URNA-directed RNA polymerase LNot AvailableHPIV-2
UEctonucleotide pyrophosphatase/phosphodiesterase family member 1Not AvailableHumans
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
Not Available
Pathways
Not Available
Pharmacogenomic Effects/ADRs
Not Available

Interactions

Drug Interactions
Not Available
Food Interactions
Not Available

References

General References
  1. Schiff ER: Emerging strategies for pegylated interferon combination therapy. Nat Clin Pract Gastroenterol Hepatol. 2007 Jan;4 Suppl 1:S17-21. [PubMed:17235281]
External Links
ChemSpider
397669
ChEBI
134989
ChEMBL
CHEMBL2111108
Wikipedia
Taribavirin

Clinical Trials

Clinical Trials
PhaseStatusPurposeConditionsCount
2CompletedTreatmentChronic Hepatitis C Virus (HCV) Infection1
2TerminatedTreatmentChronic Hepatitis C Virus (HCV) Infection1
3CompletedTreatmentChronic Hepatitis C Virus (HCV) Infection2

Pharmacoeconomics

Manufacturers
Not Available
Packagers
Not Available
Dosage forms
Not Available
Prices
Not Available
Patents
Not Available

Properties

State
Solid
Experimental Properties
Not Available
Predicted Properties
PropertyValueSource
Water Solubility11.2 mg/mLALOGPS
logP-2ALOGPS
logP-2.5ChemAxon
logS-1.3ALOGPS
pKa (Strongest Acidic)12.42ChemAxon
pKa (Strongest Basic)5.34ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count8ChemAxon
Hydrogen Donor Count5ChemAxon
Polar Surface Area150.5 Å2ChemAxon
Rotatable Bond Count3ChemAxon
Refractivity77.17 m3·mol-1ChemAxon
Polarizability22.59 Å3ChemAxon
Number of Rings2ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleNoChemAxon
Predicted ADMET features
Not Available

Spectra

Mass Spec (NIST)
Not Available
Spectra
SpectrumSpectrum TypeSplash Key
Predicted GC-MS Spectrum - GC-MSPredicted GC-MSNot Available
Predicted MS/MS Spectrum - 10V, Positive (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 20V, Positive (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 40V, Positive (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 10V, Negative (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 20V, Negative (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 40V, Negative (Annotated)Predicted LC-MS/MSNot Available

Taxonomy

Description
This compound belongs to the class of organic compounds known as triazole ribonucleosides and ribonucleotides. These are nucleoside derivatives containing a ribose (or deoxyribose) moiety which is N-glycosylated to a triazole. Nucleotides have a phosphate group linked to the C5 carbon of the ribose (or deoxyribose) moiety.
Kingdom
Organic compounds
Super Class
Nucleosides, nucleotides, and analogues
Class
Triazole ribonucleosides and ribonucleotides
Sub Class
Not Available
Direct Parent
Triazole ribonucleosides and ribonucleotides
Alternative Parents
Glycosylamines / Pentoses / Triazoles / Tetrahydrofurans / Heteroaromatic compounds / Secondary alcohols / Oxacyclic compounds / Carboximidamides / Carboxamidines / Azacyclic compounds
show 3 more
Substituents
N-ribosyl-1,2,4-triazole / Glycosyl compound / N-glycosyl compound / Pentose monosaccharide / Monosaccharide / Azole / Tetrahydrofuran / Triazole / 1,2,4-triazole / Heteroaromatic compound
show 16 more
Molecular Framework
Aromatic heteromonocyclic compounds
External Descriptors
Not Available

Targets

Kind
Protein
Organism
Influenza A virus (strain A/Beijing/11/1956 H1N1)
Pharmacological action
Unknown
General Function
Rna-directed rna polymerase activity
Specific Function
RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' met...
Gene Name
PB1
Uniprot ID
P16502
Uniprot Name
RNA-directed RNA polymerase catalytic subunit
Molecular Weight
86534.5 Da
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Nucleotide binding
Specific Function
May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-mo...
Gene Name
NT5C2
Uniprot ID
P49902
Uniprot Name
Cytosolic purine 5'-nucleotidase
Molecular Weight
64969.2 Da
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Rna binding
Specific Function
Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore pl...
Gene Name
IMPDH1
Uniprot ID
P20839
Uniprot Name
Inosine-5'-monophosphate dehydrogenase 1
Molecular Weight
55405.365 Da
4. DNA
Kind
Nucleotide
Organism
Humans
Pharmacological action
Unknown
General Function:
Used for biological information storage.
Specific Function:
DNA contains the instructions needed for an organism to develop, survive and reproduce.
Molecular Weight:
2.15 x 1012 Da
Kind
Protein
Organism
HPIV-2
Pharmacological action
Unknown
General Function
Rna-directed rna polymerase activity
Specific Function
Displays RNA-directed RNA polymerase, mRNA guanylyl transferase, mRNA (guanine-N(7)-)-methyltransferase and poly(A) synthetase activities. The viral mRNA guanylyl transferase displays a different b...
Gene Name
L
Uniprot ID
P26676
Uniprot Name
RNA-directed RNA polymerase L
Molecular Weight
256380.115 Da
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Zinc ion binding
Specific Function
By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapat...
Gene Name
ENPP1
Uniprot ID
P22413
Uniprot Name
Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Molecular Weight
104923.58 Da

Drug created on March 19, 2008 10:29 / Updated on June 04, 2019 06:23