41167-59-3

Upstream product

• 553-90-2 Dimethyl oxalate 
• 99-91-2 para-chloroacetophenone 
• 124-41-4 sodium methylate 
• 95-92-1 oxalic acid diethyl ester 
• 67-56-1 methanol 

Downstream Products

• 113416-22-1 (Z)-4-(4-Chloro-phenyl)-4-oxo-2-phenylamino-but-2-enoic acid methyl ester 
• 1276115-73-1 1-allyl-4-(4-chlorobenzoyl)-3-hydroxy-5-(4-trifluoromethylphenyl)-1,5-dihydropyrrol-2-one 
• 1276115-77-5 4-(4-chlorobenzoyl)-5-(3-fluoro-4-trifluoromethylphenyl)-3-hydroxy-1-(3-methoxypropyl)-1,5-dihydropyrrol-2-one 
• 1276115-70-8 4-(4-chlorobenzoyl)-3-hydroxy-1-(2-hydroxypropyl)-5-(4-isopropylphenyl)-1,5-dihydropyrrol-2-one 
• 425398-43-2 C₂₃H₁₉BrClN₃O₃ 

Relevant academic research and scientific papers

Design, syntheses and antitumor activities evaluation of 1,5-diaryl substituted pyrazole secnidazole ester derivatives

According to the drug hybridization principle, a series of novel 1,5-diaryl substituted pyrazole secnidazole ester derivatives (6aa–6gc) have been synthesized by the combinations of various 1,5-diarylpyrazole-3-carboxylic acids with secnidazole. The in vi

Design and biological evaluation of novel hybrids of 1, 5-diarylpyrazole and Chrysin for selective COX-2 inhibition

The overexpress of COX-2 was clearly associated with carcinogenesis and COX-2 as a possible target has long been exploited for cancer therapy. In this work, we described the design and synthesis of a series of diarylpyrazole derivatives integrating with c

Design, synthesis and structure–activity relationship of 4,5-dihydropyrrolo[3,4-c]pyrazol-6(1H)-ones as potent p53-MDM2 inhibitors

In the past decade, the p53-MDM2 protein–protein interaction by small molecules has been confirmed as a successful strategy for cancer therapy. In our previous work, pyrrolo[3,4-c]pyrazol-6(1H)-ones were found to be potent p53-MDM2 inhibitors. Further optimization and structure–activity relationship studies were described in the present work. The result revealed that benzyl group on position N1 of imidazole and bromine on C4-phenyl of pyrrolidone showed higher inhibitory activities. In vitro antiproliferative assay demonstrated the potent p53-MDM2 inhibitor 5c with 4-fold selectivity for U2 OS and Saos-2 cells. These data indicated that 4,5-dihydropyrrolo[3,4-c]pyrazol-6(1H)-one moiety is a valuable scaffold for further development of p53-MDM2 inhibitors.

Synthesis of novel hybrids of pyrazole and coumarin as dual inhibitors of COX-2 and 5-LOX

In our previous study, we designed a series of pyrazole derivatives as novel COX-2 inhibitors. In order to obtain novel dual inhibitors of COX-2 and 5-LOX, herein we designed and synthesized 20 compounds by hybridizing pyrazole with substituted coumarin w

Discovery, synthesis, and biological evaluation of orally active pyrrolidone derivatives as novel inhibitors of p53-MDM2 protein-protein interaction

The p53-MDM2 interaction has been proved to be a valuable target to develop effective antitumor agents. Novel p53-MDM2 inhibitors bearing pyrrolidone scaffolds were successfully identified by structure-based design. The nanomolar inhibitor 5 possessed good p53-MDM2 inhibitory activity (Ki = 780 nM) due to its hydrophobic and hydrogen bonding interactions with MDM2. Further hit optimization led to the discovery of a number of highly potent pyrrolidone derivatives with improved p53-MDM2 inhibitory activity and in vitro antiproliferative potency. Compounds 41 (Ki = 260.0 nM) and 60a (Ki = 150.0 nM) showed good and selective activity against tumor cells with deleted p53. In addition, these two compounds also effectively inhibited the tumor growth in the A549 xenograft model. Interestingly, compound 41 was proved to be a potent MDM2/MDMX dual inhibitor. The novel pyrrolidone p53-MDM2 inhibitors represent promising lead structures for the development of novel antitumor agents.

Design, synthesis, and structure-activity relationship exploration of 1-substituted 4-aroyl-3-hydroxy-5-phenyl-1 H -pyrrol-2(5 H)-one analogues as inhibitors of the annexin A2′S100A10 protein interaction

S100 proteins are small adaptors that regulate the activity of partner proteins by virtue of direct protein interactions. Here, we describe the first small molecule blockers of the interaction between S100A10 and annexin A2. Molecular docking yielded cand