700372-76-5

Upstream product

• 5703-26-4 4-Methoxyphenylacetaldehyde 
• 3353-51-3 2-(4-methoxyphenyl)acetaldehyde oxime 
• 3179-10-0 1-methoxy-4-(2-nitro-vinyl)-benzene 

Downstream Products

• 1253183-41-3 tert-butyl 3-(4-methoxybenzyl)-6,6a-dihydro-3aH-pyrrolo[ 3,4-d]isoxazole-5(4H)-carboxylate 
• 1338733-17-7 3-(4-methoxybenzyl)-5-methyl-4,5,6,6a-tetrahydro-3aH-pyrrolo-[3,4-d]isoxazole oxalate 
• 1338733-02-0 3-(4-methoxybenzyl)-5-methyl-4,5,6,6a-tetrahydro-3aH-pyrrolo-[3,4-d]isoxazole 

Relevant academic research and scientific papers

An expeditious synthesis of an analogue of (-)-steviamine by way of the 1,3-dipolar cycloaddition of a nitrile oxide with a 1-C-allyl iminosugar

In our continuing effort to develop inhibitors of the mycobacterial galactan biosynthesis, we planned to synthesize original iminosugar-based analogues of UDP-galactofuranose by way of the 1,3-dipolar cycloaddition reaction between a 1-C-allyl iminosugar and a nitrile oxide, followed by the reductive cleavage of the resulting isooxazoline. In initial studies, it was found that this last step led in one pot to a new poly-hydroxylated indolizidine derivative closely related to the recently isolated (-)-steviamine, in good yield, by way of a sequence involving at least five individual reactions. The activity of this new compound as a glycosidase inhibitor was evaluated against a panel of glycosidases and compared to (-)-steviamine.

Synthesis and biochemical evaluation of δ2-isoxazoline derivatives as DNA methyltransferase 1 inhibitors

A series of Δ2-isoxazoline constrained analogues of procaine/procainamide (7a-k and 8a-k) were prepared and their inhibitory activity against DNA methyltransferase 1 (DNMT1) was tested. Among them, derivative 7b is far more potent in vitro (IC50 = 150 μM) than other non-nucleoside inhibitors and also exhibits a strong and dose-dependent antiproliferative effect against HCT116 human colon carcinoma cells. The binding mode of 7b with the enzyme was also investigated by means of a simple competition assay as well as of docking simulations conducted using the recently published crystallographic structure of human DNMT1. On the basis of the findings, we assessed that the mode of inhibition of 7b is consistent with a competition with the cofactor and propose it as a novel lead compound for the development of non-nucleoside DNMT inhibitors.