113458-95-0

Basic information

• Product Name: 2-Naphthalenecarboxylic acid, 6,7-dihydroxy- (9CI)
• Synonyms: 2-Naphthalenecarboxylic acid, 6,7-dihydroxy- (9CI)
• CAS NO: 113458-95-0
• Molecular Formula: C₁₁H₈O₄
• Molecular Weight: 204.17882
• Product Categories: ALCOHOL
• Mol File: 113458-95-0.mol
• Article Data: 6

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 2-Naphthalenecarboxylic acid, 6,7-dihydroxy- (9CI)(CAS DataBase Reference)
• NIST Chemistry Reference: 2-Naphthalenecarboxylic acid, 6,7-dihydroxy- (9CI)(113458-95-0)
• EPA Substance Registry System: 2-Naphthalenecarboxylic acid, 6,7-dihydroxy- (9CI)(113458-95-0)

Safety Data

• Hazardous Substances Data: 113458-95-0(Hazardous Substances Data)

Upstream product

• 37707-78-1 6,7-Dimethoxy-naphthalene-2-carboxylic Acid 
• 72337-67-8 6,7-dimethoxy-2-naphthalenecarbonyl chloride 
• 16712-64-4 6-Hydroxy-2-naphthoic acid 
• 10103-06-7 2,3-dimethoxynaphthalene 
• 37707-72-5 6,7-dimethoxy-2-acetylnaphthalene 
• 146515-37-9 6,7-dihydroxy-2-naphthalenecarboxamide 

Downstream Products

• 188662-02-4 6,7-Dihydroxy-naphthalene-2-carboxylic acid pentafluorophenyl ester 
• 169232-18-2 6,7-Dihydroxy-2-naphthoic acid β-phenylethyl ester 

Relevant articles and documents

Biocatalytic synthesis of dihydroxynaphthoic acids by cytochrome P450 CYP199A2

CYP199A2, a bacterial P450 monooxygenase from Rhodopseudomonas palustris, was found to exhibit oxidation activity towards three hydroxynaphthoic acids. Whole cells of the recombinant Escherichia coli strain expressing CYP199A2 efficiently catalyzed the re

Derivatives of naphthalene with comt inhibiting activity

Compounds of formula (I′), wherein A, R1 to R3 and t are as defined in the disclosure, exhibit COMT enzyme inhibiting activity so that they are useful as COMT inhibitors.

Hydroxylated aromatic inhibitors of HIV-1 integrase

Efficient replication of HIV-1 requires integration of a DNA copy of the viral genome into a chromosome of the host cell. Integration is catalyzed by the viral integrase, and we have previously reported that phenolic moieties in compounds such as flavones, caffeic acid phenethyl ester (CAPE, 2), and curcumin confer inhibitory activity against HIV-1 integrase. We now extend these findings by performing a comprehensive structure-activity relationship using CAPE analogues. Approximately 30 compounds have been prepared as HIV integrase inhibitors based on the structural lead provided by CAPE, which has previously been shown to exhibit an IC50 value of 7 μM in our integration assay. These analogues were designed to examine specific features of the parent CAPE structure which may be important for activity. Among the features examined for their effects on inhibitory potency were ring substitution, side chain length and composition, and phenyl ring conformational orientation. In an assay which measured the combined effect of two sequential steps, dinucleotide cleavage and strand transfer, several analogues have IC50 values for 3'-processing and strand transfer lower than those of CAPE. Inhibition of strand transfer was assayed using both blunt-ended and 'precleaved' DNA substrates. Disintegration using an integrase mutant lacking the N-terminal zinc finger and C-terminal DNA-binding domains was also inhibited by these analogues, suggesting that the binding site for these compounds resides in the central catalytic core. Several CAPE analogues were also tested for selective activity against transformed cells. Taken together, these results suggest that the development of novel antiviral agents for the treatment of acquired immune deficiency syndrome can be based upon inhibition of HIV-1 integrase.