306990-93-2

Basic information

• Product Name: (1H-benzo[d][1,2,3]triazol-1-yl)(2-methoxyphenyl)methanone
• Synonyms: (1H-benzo[d][1,2,3]triazol-1-yl)(2-methoxyphenyl)methanone
• CAS NO: 306990-93-2
• Molecular Weight: 253.26
• Mol File: 306990-93-2.mol
• Article Data: 16

Chemical Properties

• CAS DataBase Reference: (1H-benzo[d][1,2,3]triazol-1-yl)(2-methoxyphenyl)methanone(CAS DataBase Reference)
• NIST Chemistry Reference: (1H-benzo[d][1,2,3]triazol-1-yl)(2-methoxyphenyl)methanone(306990-93-2)
• EPA Substance Registry System: (1H-benzo[d][1,2,3]triazol-1-yl)(2-methoxyphenyl)methanone(306990-93-2)

Safety Data

• Hazardous Substances Data: 306990-93-2(Hazardous Substances Data)

Upstream product

• 579-75-9 2-Methoxybenzoic acid 
• 37073-15-7 1-(methanesulfonyl)-1H-1,2,3-benzotriazole 
• 95-14-7 1,2,3-Benzotriazole 
• 123-11-5 4-methoxy-benzaldehyde 
• 21615-34-9 2-Methoxybenzoyl chloride 

Downstream Products

• 6706-92-9 2,2'-dimethoxybenzil 
• 51892-24-1 2-Methoxy-thiobenzoesaeure-S-phenylester 
• 101093-59-8 S-benzyl 2-methoxybenzenecarbothioate 
• 820234-17-1 (1H-indol-1-yl)(2-methoxyphenyl)methanone 
• 1260613-32-8 1-(2-methoxybenzoyl)imidazolidin-2-one 
• 1043910-90-2 C₅₃H₆₃N₅O₈ 
• 1043910-19-5 3-demethoxycarbonyl-3-(2'-methoxybenzoylamino)methylvindoline 
• 1226-63-7 1,3-bis(2-methoxyphenyl)urea 
• 6833-21-2 2-methoxy-N-phenylbenzamide 
• 95461-02-2 N-phenyl-N'-(2-methoxybenzenecarbonyl)urea 
• 13142-82-0 N-(2-methoxyphenyl)-N'-phenyl-urea 
• 60681-96-1 2-(2-methoxyphenyl)-4H-benzo[d][1,3]oxazin-4-one 
• 46270-50-2 1-(2-methoxyphenyl)-2-nitroethan-1-one 

Relevant articles and documents

Nickel-Catalyzed Reductive Cross-Coupling of N-Acyl and N-Sulfonyl Benzotriazoles with Diverse Nitro Compounds: Rapid Access to Amides and Sulfonamides

Herein we report a Ni-catalyzed reductive transamidation of conveniently available N-acyl benzotriazoles with alkyl, alkenyl, and aryl nitro compounds, which afforded various amides with good yields and a broad substrate scope. The same catalytic reaction conditions were also applicable for N-sulfonyl benzotriazoles, which could undergo smooth reductive coupling with nitroarenes and nitroalkanes to afford the corresponding sulfonamides.

Trichloroisocyanuric Acid Mediated High-Yielding Synthesis of N -Acylbenzotriazoles under Mild Reaction Conditions

N -Acylbenzotriazoles are achieved in good yields from the corresponding carboxylic acids by using only 0.35 equivalent of trichloroisocyanuric acid and 1.2 equivalents of PPh 3. The salient features of the developed reaction path include an ec

Synthesis of benzotriazoles derivatives and their dual potential as α-amylase and α-glucosidase inhibitors in vitro: Structure-activity relationship, molecular docking, and kinetic studies

Benzotriazoles (4–6) were synthesized which were further reacted with different substituted benzoic acids and phenacyl bromides to synthesize benzotriazole derivatives (7–40). The synthetic compounds (7–40) were characterized via different spectroscopic techniques including EI-MS, HREI-MS, 1H-, and 13C NMR. These molecules were examined for their anti-hyperglycemic potential hence were evaluated for α-glucosidase and α-amylase inhibitory activities. All benzotriazoles displayed moderate to good inhibitory activity in the range of IC50 values of 2.00–5.6 and 2.04–5.72 μM against α-glucosidase and α-amylase enzymes, respectively. The synthetic compounds were divided into two categories “A” and “B”, in order to understand the structure-activity relationship. Compounds 25 (IC50 = 2.41 ± 1.31 μM), (IC50 = 2.5 ± 1.21 μM), 36 (IC50 = 2.12 ± 1.35 μM), (IC50 = 2.21 ± 1.08 μM), and 37 (IC50 = 2.00 ± 1.22 μM), (IC50 = 2.04 ± 1.4 μM) with chloro substitution/s at aryl ring were found to be most active against α-glucosidase and α-amylase enzymes. Molecular docking studies on all compounds were performed which revealed that chloro substitutions are playing a pivotal role in the binding interactions. The enzyme inhibition mode was also studied and the kinetic studies revealed that the synthetic molecules have shown competitive mode of inhibition against α-amylase and non-competitive mode of inhibition against α-glucosidase enzyme.