74426-51-0Relevant articles and documents
Preparation method of N-phenylacetyl-2-hydroxymethylpyrrolidine-2-formamide and medicinal application of N-phenylacetyl-2-hydroxymethylpyrrolidine-2-formamide
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Paragraph 0042; 0043, (2021/01/12)
The invention discloses N-phenylacetyl-2-hydroxymethylpyrrolidine-2-formamide as shown in a general formula (I), a preparation method of the compound, a new application of the compound and a pharmaceutical composition containing the compound in the aspect of inhibiting neuroglial cell inflammation. Wherein R1/R2 is equal to H, F, CF3 or OCF3.
Discovery of pyrrolo[2,3-d]pyrimidine derivatives as potent Axl inhibitors: Design, synthesis and biological evaluation
Xu, Dandan,Sun, Deqiao,Wang, Wei,Peng, Xia,Zhan, Zhengsheng,Ji, Yinchun,Shen, Yanyan,Geng, Meiyu,Ai, Jing,Duan, Wenhu
, (2021/05/06)
Axl has emerged as an attractive target for cancer therapy due to its strong correlation with tumor growth, metastasis, poor survival, and drug resistance. Herein, we report the design, synthesis and structure-activity relationship (SAR) investigation of a series of pyrrolo[2,3-d]pyrimidine derivatives as new Axl inhibitors. Among them, the most promising compound 13b showed high enzymatic and cellular Axl potencies. Furthermore, 13b possessed preferable pharmacokinetic properties and displayed promising therapeutic effect in BaF3/TEL-Axl xenograft tumor model. Compound 13b may serve as a lead compound for new antitumor drug discovery.
Phosphonic acid analogs of fluorophenylalanines as inhibitors of human and porcine aminopeptidases N: Validation of the importance of the substitution of the aromatic ring
Dziuk, B?a?ej,Kafarski, Pawe?,Pirat, Jean-Luc,Talma, Micha?,Wanat, Weronika
, (2020/05/04)
A library of phosphonic acid analogs of phenylalanine substituted with fluorine, chlorine and trifluoromethyl moieties on the aromatic ring was synthesized and evaluated for inhibitory activity against human (hAPN) and porcine (pAPN) aminopeptidases. Fluorogenic screening indicated that these analogs are micromolar or submicromolar inhibitors, both enzymes being more active against hAPN. In order to better understand the mode of the action of the most active compounds, molecular modeling was used. It confirmed that aminophosphonic portion of the enzyme is bound nearly identically in the case of all the studied compounds, whereas the difference in activity results from the placement of aromatic side chain of an inhibitor. Interestingly, both enantiomers of the individual compounds are usually bound quite similarly.