Unequivocal structural assignment of the product of methylation of 4-nitro-5-styrylimidazole

Vaidya, Vijayvithal P.; Hosmane, Ramachandra S.; Siriwardane, Upali; Zhang, Hongming; Hosmane, Narayan S.

doi:10.1007/bf00681209

Cited by 4 publications

(2 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Compound 2 was obtained as a single regioisomer as determined from NMR data. The regioisomeric assignment of 2 was based upon (a) comparison of the benzyl absorptions of 2 in its 1 H NMR spectrum with those of several other benzylsubstituted nitroimidazoles previously synthesized in this laboratory [3][4][5], and (b) the established fact that the alkylation of nitroimidazoles predominantly yield substitutions at the nitrogen atom farther away from the nitro group [6].…”

Section: Resultsmentioning

confidence: 99%

Synthetic Analogue of Stilbene Containing an Imidazole Nucleus

Siddiqui

Hosmane

2000

Molecules

View full text Add to dashboard Cite

Synthesis of trans-1, 2-bis(4-nitro-1-p-methoxybenzylimidazol-5-yl)ethene (1) as an imidazole analogue of stilbene has been reported. In order to confirm the trans geometry of the product using an UV spectral comparison, a mixture of both trans (1) and cis isomer (3) was also prepared. The synthesis involved one-step dimerization of the precursor, 4-nitro-1-p-methoxybenzyl-5-methyl-1H-imidazole (2), using N-chlorosuccinimide catalyzed by potassium t-butoxide.

show abstract

Section: Resultsmentioning

confidence: 99%

Synthetic Analogue of Stilbene Containing an Imidazole Nucleus

Siddiqui

Hosmane

2000

Molecules

View full text Add to dashboard Cite

show abstract

“…This regioisomeric structural assignment based on the 1 H NMR data has further been corroborated by single crystal X-ray diffraction analysis of 1-methyl-4-nitro-5-styrylimidazole reported from this laboratory. 38 Finally, oxidation of the 19a and 19b with aqueous potassium permanganate gave the desired 16a and 16b , in 61% and 58% yields, respectively.…”

Section: Chemistrymentioning

confidence: 97%

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

Tantravedi

Chakraborty

Shah

et al. 2013

Bioorganic & Medicinal Chemistry

Self Cite

View full text Add to dashboard Cite

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 enzymecatalyzed 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 M against rabbit liver guanase.

show abstract