4664-65-7

Upstream product

• 108-86-1 bromobenzene 
• 121-33-5 vanillin 
• 916793-29-8 (3-methoxy-4-(4-nitrophenoxy)phenyl)methanol 
• 350-46-9 4-Fluoronitrobenzene 
• 166904-09-2 3-methoxy-4-(4-nitrophenoxy)benzaldehyde 
• 2426-87-1 3-methoxy-4-(phenylmethoxy)benzaldehyde 

Downstream Products

• 4664-62-4 3-methoxy-4-benzoxybenzaldehyde 
• 875246-01-8 3-methoxy-4-phenoxybenzoic acid 
• 129623-63-8 3-hydroxy-4-phenoxy-benzoic acid 
• 35065-13-5 3-hydroxy-4-phenoxybenzaldehyde 

Relevant academic research and scientific papers

Design, synthesis, and activity evaluation of novel N-benzyl deoxynojirimycin derivatives for use as α-glucosidase inhibitors

To obtain α-glucosidase inhibitors with high activity, 19 NB-DNJDs (N-benzyldeoxynojirimycin derivatives) were designed and synthesized. The results indicated that the 19 NBDNJDs displayed different inhibitory activities towards α-glucosidase in vitro. Compound 18a (1- (4-hydroxy-3-methoxybenzyl)-2-(hydroxymethyl) piperidine-3,4,5-triol) showed the highest activity, with an IC50 value of 0.207 ± 0.11 mM, followed by 18b (1-(3-bromo-4-hydroxy-5- methoxybenzyl)-2-(hydroxymethyl) piperidine-3,4,5-triol, IC50: 0.276 ± 0.13 mM). Both IC50 values of 18a and 18b were significantly lower than that of acarbose (IC50: 0.353 ± 0.09 mM). According to the structure-activity analysis, substitution of the benzyl and bromine groups on the benzene ring decreased the inhibition activity, while methoxy and hydroxyl group substitution increased the activity, especially with the hydroxyl group substitution. Molecular docking results showed that three hydrogen bonds were formed between compound 18a and amino acids in the active site of α- glucosidase. Additionally, an arene-arene interaction was also modelled between the phenyl ring of compound 18a and Arg 315. The three hydrogen bonds and the arene-arene interaction resulted in a low binding energy (-5.8 kcal/mol) and gave 18a a higher inhibition activity. Consequently, compound 18a is a promising candidate as a new α-glucosidase inhibitor for the treatment of type II diabetes.

Novel diphenyl ethers: Design, docking studies, synthesis and inhibition of enoyl ACP reductase of Plasmodium falciparum and Escherichia coli

We designed some novel diphenyl ethers and determined their binding energies for Enoyl-Acyl Carrier Protein Reductase (ENR) of Plasmodium falciparum using Autodock. Out of these, we synthesized the promising compounds and tested them for their inhibitory