3743-69-9

Upstream product

• 95-55-6 2-amino-phenol 
• 122-59-8 2-phenoxyacetic acid 
• 701-99-5 Phenoxyacetyl chloride 

Downstream Products

• 1469268-19-6 tert-butyl 2-[2-(2-{2-[2-(2-phenoxyacetamido)phenoxy]acetamido}ethoxy)ethoxy]ethylcarbamate 
• 1469268-04-9 5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-N-{2-[2-(2-{2-[2-(2-phenoxyacetamido)phenoxy]acetamido}ethoxy)ethoxy]ethyl}pentanamide 
• 7506-48-1 2-(phenoxymethyl)benzo[d]oxazole 

Relevant academic research and scientific papers

Synthesis and structure-activity relationship study of chemical probes as hypoxia induced factor-1α/malate dehydrogenase 2 inhibitors

A structure-activity relationship study of hypoxia inducible factor-1α inhibitor 3-aminobenzoic acid-based chemical probes, which were previously identified to bind to mitochondrial malate dehydrogenase 2, was performed to provide a better understanding of the pharmacological effects of LW6 and its relation to hypoxia inducible factor-1α (HIF-1α) and malate dehydrogenase 2 (MDH2). A variety of multifunctional probes including the benzophenone or the trifluoromethyl diazirine for photoaffinity labeling and click reaction were prepared and evaluated for their biological activity using a cell-based HRE-luciferase assay as well as a MDH2 assay in human colorectal cancer HCT116 cells. Among them, the diazirine probe 4a showed strong inhibitory activity against both HIF-1α and MDH2. Significantly, the inhibitory effect of the probes on HIF-1α activity was consistent with that of the MDH2 enzyme assay, which was further confirmed by the effect on in vitro binding activity to recombinant human MDH2, oxygen consumption, ATP production, and AMP activated protein kinase (AMPK) activation. Competitive binding modes of LW6 and probe 4a to MDH2 were also demonstrated.

Identification of malate dehydrogenase 2 as a target protein of the HIF-1 inhibitor LW6 using chemical probes

Tracking the target: To identify a protein that binds directly to the HIF-1α inhibitor LW6, a series of new chemical probes were synthesized with a clickable tag and/or a photoactivatable moiety. LW6 was found to be localized to the mitochondria (see picture) and MDH2 was identified as a target protein of LW6. These results indicate that the HIF-1α inhibitory activity of LW6 is a consequence of MDH2 suppression. Copyright

A microwave assisted synthesis of benzoxazoles from carboxylic acids

A series of various poly-substituted benzoxazoles were synthesized starting from readily available carboxylic acids. The method is based on TCT (cyanuric chloride)/microwave acid activation and it is characterized by mild conditions, allowing for a wide range of starting materials and functionalization of final products.

Synthesis and microbiological activity of some novel N-(2-hydroxyl-5- substitutedphenyl)benzacetamides, phenoxyacetamides and thiophenoxyacetamides as the possible metabolites of antimicrobial active benzoxazoles

Synthesis of some novel N-(2-hydroxyl-5- substitutedphenyl)benzacetamides, phenoxyacetamides and thiophenoxyacetamides (5a-k) were described in order to determine their in vitro antimicrobial activity against 3 Gram-positive, 3 Gram-negative bacteria and the fungus Candida albicans comparing with several control drugs. The derivative 5e was found active at a MIC value of 25μg/ml against the whole tested Gram- positive bacteria strains and the Gram-negative microorganism Klebsiella pneumoniae. Moreover, the synthesized compounds 5a-k exhibited significant antibacterial activity against the enterobacter Pseudomonas aureginosae when compared to the control drugs. For the antifungal activity against C. albicans, the compound 5k was found more active than the other synthesized derivatives. On the other hand, the antimicrobial activity of some of these acetamide derivatives (5c, 5d, 5e, 5j and 5k) which are the possible metabolites of benzoxazoles, were also compared with their cyclic analogues 6-10. However, most of the MIC values of the benzoaxazole derivatives provided better activity than the compared acetamides, while some others of the acetamide derivatives possessed either one fold improved (5d, 5e and 5j) or the same potency (5c, 5d, 5e, 5j and 5k) against the tested microorganisms.