776-47-6Relevant articles and documents
Synthesis and dyeing properties of indophenine dyes for polyester fabrics
Jiang, Hua,Hu, Qian,Cai, Jinfang,Cui, Zhihua,Zheng, Jinhuan,Chen, Weiguo
, p. 130 - 139 (2019)
In this study, a series of indophenine dyes (D1-D6) that show high molecular planarity, were synthesized and applied as dyeing materials for poly (ethylene terephthalate) fabrics. The relationship between the dye molecular structure and dyeing properties, such as dyeing rate and color fastness properties, was investigated. Compared with conventional azo or anthraquinone dyes, the indophenine dyes had a much lower dyeing rate but very good anti-thermomigration properties. This phenomenon indicated that there exists much larger intermolecular interaction between indophenine dye molecules, which was also confirmed by the results of quantum chemical density functional theory (DFT) calculations. The substituent effect of alkyl groups and halogen atoms (F and Cl) was also investigated. The steric hindrance of linked ethyl groups could efficiently promote dyeing performance, while halogen atoms lowered the color acquisition. As a result, D4 with only two N-ethyl groups incorporated on the indophenine backbone showed the best overall dyeing performance.
Deglycase-activity oriented screening to identify DJ-1 inhibitors
David, Yael,Finkin-Groner, Efrat,Fukase, Yoshiyuki,Huggins, David J.,Maksimovic, Igor,Michino, Mayako,Myers, Robert W.,Sun, Shan,Zheng, Qingfei
supporting information, p. 1232 - 1238 (2021/09/28)
The oncoprotein and Parkinson's disease-associated enzyme DJ-1/PARK7 has emerged as a promiscuous deglycase that can remove methylglyoxal-induced glycation adducts from both proteins and nucleotides. However, dissecting its structural and enzymatic functions remains a challenge due to the lack of potent, specific, and pharmacokinetically stable inhibitors targeting its catalytic site (including Cys106). To evaluate potential drug-like leads against DJ-1, we leveraged its deglycase activity in an enzyme-coupled, fluorescence lactate-detection assay based on the recent understanding of its deglycation mechanism. In addition, we developed assays to directly evaluate DJ-1's esterase activity using both colorimetric and fluorescent substrates. The resulting optimized assay was used to evaluate a library of potential reversible and irreversible DJ-1 inhibitors. The deglycase activity-oriented screening strategy described herein establishes a new platform for the discovery of potential anti-cancer drugs.
Design, synthesis, and biological evaluation of 1,2,3-triazole-linked triazino[5,6-b]indole-benzene sulfonamide conjugates as potent carbonic anhydrase I, II, IX, and XIII inhibitors
Angeli, Andrea,Arifuddin, Mohammed,Biswas, Rashmita,Chinchilli, Krishna Kartheek,Korra, Laxman Naik,Supuran, Claudiu T.,Thacker, Pavitra S.
, (2020/06/17)
A series of 1,2,3-triazole-linked triazino[5,6-b]indole-benzene sulfonamide hybrids (6a– 6o) was synthesized and evaluated for carbonic anhydrase (CA, EC 4.2.1.1) inhibitory activity against the human (h) isoforms hCA I, II, XIII (cytosolic isoforms), and hCA IX (transmembrane tumor-associated isoform). The results revealed that the compounds 6a–6o exhibited Ki values in the low to medium nanomolar range against hCA II and hCA IX (Kis ranging from 7.7 nM to 41.3 nM) and higher Ki values against hCA I and hCA XIII. Compound 6i showed potent inhibition of hCA II (Ki = 7.7nM), being more effective compared to the standard inhibitor acetazolamide (AAZ) (Ki = 12.1 nM). Compounds 6b and 6d showed moderate activity against hCA XIII (Ki= 69.8 and 65.8 nM). Hence, compound 6i could be consider as potential lead candidate for the design of potent and selective hCA II inhibitors.
