1274572-86-9

Basic information

• Product Name: C₁₇H₁₈N₂O₆
• Synonyms: C₁₇H₁₈N₂O₆
• CAS NO: 1274572-86-9
• Molecular Weight: 346.34
• Mol File: 1274572-86-9.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: C₁₇H₁₈N₂O₆(CAS DataBase Reference)
• NIST Chemistry Reference: C₁₇H₁₈N₂O₆(1274572-86-9)
• EPA Substance Registry System: C₁₇H₁₈N₂O₆(1274572-86-9)

Safety Data

• Hazardous Substances Data: 1274572-86-9(Hazardous Substances Data)

Upstream product

• 13130-13-7 5-(3-nitro-phenyl)-furan-2-carboxylic acid 
• 15678-99-6 N-tert-butylchloroacetamide 

Relevant articles and documents

Structural and biochemical study on the inhibitory activity of derivatives of 5-nitro-furan-2-carboxylic acid for RNase H function of HIV-1 reverse transcriptase

Rapid emergence of drug-resistant variants is one of the most serious problems in chemotherapy for HIV-1 infectious diseases. Inhibitors acting on a target not addressed by approved drugs are of great importance to suppress drug-resistant viruses. HIV-1 reverse transcriptase has two enzymatic functions, DNA polymerase and RNase H activities. The RNase H activity is an attractive target for a new class of antiviral drugs. On the basis of the hit chemicals found in our previous screening with 20,000 small molecular-weight compounds, we synthesized derivatives of 5-nitro-furan-2-carboxylic acid. Inhibition of RNase H enzymatic activity was measured in a biochemical assay with real-time monitoring of florescence emission from the digested RNA substrate. Several derivatives showed higher inhibitory activities that those of the hit chemicals. Modulation of the 5-nitro-furan-2-carboxylic moiety resulted in a drastic decrease in inhibitory potency. In contrast, many derivatives with modulation of other parts retained inhibitory activities to varying degrees. These findings suggest the binding mode of active derivatives, in which three oxygen atoms aligned in a straight form at the nitro-furan moiety are coordinated to two divalent metal ions located at RNase H reaction site. Hence, the nitro-furan-carboxylic moiety is one of the critical scaffolds for RNase H inhibition. Of note, the RNase H inhibitory potency of a derivative was improved by 18-fold compared with that of the original hit compound, and no significant cytotoxicity was observed for most of the derivatives showing inhibitory activity. Since there is still much room for modification of the compounds at the part opposite the nitro-furan moiety, further chemical conversion will lead to improvement of compound potency and specificity.