6307-17-1

Basic information

• Product Name: 1H-IMIDAZOLE, 4-NITRO-5-[(E)-2-PHENYLETHENYL]-
• Synonyms: 4-NITRO-5-STYRYL IMIDAZOLE;1H-IMIDAZOLE, 4-NITRO-5-[(E)-2-PHENYLETHENYL]-;4-nitro-5-(2-phenylethenyl)-1h-imidazol;4-Nitro-5-(2-phenylethenyl)-1H-imidazole
• CAS NO: 6307-17-1
• Molecular Formula: C₁₁H₉N₃O₂
• Molecular Weight: 215.21
• Mol File: 6307-17-1.mol
• Article Data: 1

Chemical Properties

• Boiling Point: 480.9°C at 760 mmHg
• Flash Point: 244.7°C
• Appearance: /
• Density: 1.379g/cm³
• Vapor Pressure: 6.07E-09mmHg at 25°C
• Refractive Index: 1.736
• CAS DataBase Reference: 1H-IMIDAZOLE, 4-NITRO-5-[(E)-2-PHENYLETHENYL]-(CAS DataBase Reference)
• NIST Chemistry Reference: 1H-IMIDAZOLE, 4-NITRO-5-[(E)-2-PHENYLETHENYL]-(6307-17-1)
• EPA Substance Registry System: 1H-IMIDAZOLE, 4-NITRO-5-[(E)-2-PHENYLETHENYL]-(6307-17-1)

Safety Data

• Hazardous Substances Data: 6307-17-1(Hazardous Substances Data)

Usage

Safety Profile

Mutation data reported. Whenheated to decomposition it emits toxic vapors of NOx.

InChI:InChI=1/C11H9N3O2/c15-14(16)11-10(12-8-13-11)7-6-9-4-2-1-3-5-9/h1-8H,(H,12,13)

Upstream product

• 14003-66-8 4-methyl-5-nitro-1H-imidazole 
• 100-52-7 benzaldehyde 

Downstream Products

• 40507-59-3 5⁽⁴⁾-nitro-1⁽³⁾H-imidazole-4⁽⁵⁾-carboxylic acid 
• 1450627-80-1 1-(4-methoxybenzyl)-5-nitro-4-styryl-1H-imidazole 
• 1450627-82-3 1-(4-methoxybenzyl)-4-nitro-5-styryl-1H-imidazole 
• 1450627-81-2 (E)-1-(4-fluorobenzyl)-5-nitro-4-styryl-1H-imidazole 
• 1450627-83-4 (E)-1-(4-fluorobenzyl)-4-nitro-5-styryl-1H-imidazole 

Relevant articles and documents

Analogs of iso-azepinomycin as potential transition-state analog inhibitors of guanase: Synthesis, biochemical screening, and structure-activity correlations of various selectively substituted imidazo[4,5-e][1,4]diazepines

Guanase is an important enzyme of the purine salvage pathway of nucleic acid metabolism and its inhibition has beneficial implications in viral, bacterial, and cancer therapy. The work described herein is based on a hypothesis that azepinomycin, a heterocyclic natural product and a purported transition state analog inhibitor of guanase, does not represent the true transition state of the enzyme-catalyzed reaction as closely as does iso-azepinomycin, wherein the 6-hydroxy group of azepinomycin has been translocated to the 5-position. Based on this hypothesis, and assuming that iso-azepinomycin would bind to guanase at the same active site as azepinomycin, several analogs of iso-azepinomycin were designed and successfully synthesized in order to gain a preliminary understanding of the hydrophobic and hydrophilic sites surrounding the guanase binding site of the ligand. Specifically, the analogs were designed to explore the hydrophobic pockets, if any, in the vicinity of N1, N3, and N4 nitrogen atoms as well as O5 oxygen atom of iso-azepinomycin. Biochemical inhibition studies of these analogs were performed using a mammalian guanase. Our results indicate that (1) increasing the hydrophobicity near O5 results in a negative effect, (2) translocating the hydrophobicity from N3 to N1 also results in decreased inhibition, (3) increasing the hydrophobicity near N3 or N4 produces significant enhancement of inhibition, (4) increasing the hydrophobicity at either N3 or N4 with a simultaneous increase in hydrophobicity at O5 considerably diminishes any gain in inhibition made by solely enhancing hydrophobicity at N3 or N4, and (5) finally, increasing the hydrophilic character near N3 has also a deleterious effect on inhibition. The most potent compound in the series has a Ki value of 8.0 ± 1.5 μM against rabbit liver guanase.