879216-18-9

Upstream product

• 39757-36-3 4-(4-Nitro-phenyl)-2,4-dioxo-butyric acid methyl ester 
• 487034-01-5 5-(4-nitro-phenyl)-isoxazole-3-carboxylic acid methyl ester 
• 100-19-6 (4-nitrophenyl)ethanone 

Downstream Products

• 879216-19-0 5-[4-(5,5-dimethyl-4-oxo-hexanoylamino)-phenyl]-isoxazole-3-carboxylic acid methyl ester 
• 879216-20-3 5-[4-(3-prop-2-ynylcarbamoyl-propionylamino)-phenyl]-isoxazole-3-carboxylic acid methyl ester 
• 879217-72-8 5-[4-(3-prop-2-ynylcarbamoyl-propionylamino)-phenyl]-isoxazole-3-carboxylic acid 

Relevant academic research and scientific papers

Synthesis and structure-activity relationship of new chalcone linked 5-phenyl-3-isoxazolecarboxylic acid methyl esters potentially active against drug resistant Mycobacterium tuberculosis

In search of novel therapeutic agents active against emerging drug-resistant Mycobacterium tuberculosis and to counter the long treatment protocol of existing drugs, herein we present synthesis and biological evaluation of a new series of 5-phenyl-3-isoxazolecarboxylic acid methyl ester-chalcone hybrids. Among 35 synthesized compounds, 32 analogues displayed potent in-vitro activity against Mycobacterium tuberculosis H37Rv with MIC 0.12–16 μg/mL. Cell viability test against Vero cells indicated 29 compounds to be non-cytotoxic (CC50 > 20 μg/mL & SI > 10). Most potent compounds with MIC 0.12 μg/mL (7 b, 7j, 7 ab) exhibited selectivity index (SI) in excess of 320. Further studies on activity against drug-resistant Mycobacterium tuberculosis revealed 7j as the most potent compound with MIC 0.03–0.5 μg/mL. Time-kill kinetic study suggested compound 7j displaying concentration-dependent bactericidal killing activity with relatively comparable potency to that of current first-line anti-TB drugs. Taken together, 7j presents a novel hit with potential to be translated into a potent antimycobacterial.

Rapid assembly and in situ screening of bidentate inhibitors of protein tyrosine phosphatases

We have successfully designed and synthesized a small library of protein tyrosine phosphatase (PTP) inhibitors, in which the so-called "click chemistry" or Cu(I)-catalyzed 1,3-dipolar alkyne-azide coupling reaction was carried out for rapid assembly of 66 different bidentate compounds. Subsequent in situ enzymatic screening revealed a potential PTP1B inhibitor (IC50 = 4.7 μM) which is 10-100 fold more potent than other PTPs.