4943-86-6Relevant articles and documents
Palladium(0)-catalysed regioselective cyclisations of 2-amino(tosyl) benzamides/sulphonamides: The stereoselective synthesis of 3-ylidene-[1,4]benzodiazepin-5-ones/benzo[f][1,2,5]thiadiazepine-1,1-dioxides
Mondal, Debasmita,Pal, Gargi,Chowdhury, Chinmay
supporting information, p. 5462 - 5465 (2021/06/09)
The Pd(0) catalysed cyclisation reactions betweentert-butyl propargyl carbonates and 2-aminotosyl benzamides or sulphonamides deliver 1,4-benzodiazepin-5-ones or sultam derivatives, key components of many biologically active compounds. But 2-amino benzamides/sulphonamides require propargyl carbonates substituted at acetylenic carbon to undergo the reaction resulting in the stereoselective formation of the said products.
MODIFIED PROTEINS AND PROTEIN DEGRADERS
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Paragraph 00508-00510, (2021/12/08)
Provided herein are compounds, pharmaceutical compositions, and methods for binding or degrading target proteins. Further provided herein are compounds having a DNA damage-binding protein 1 (DDB1) binding moiety. Some such embodiments include a linker. Some such embodiments include a target protein binding moiety. Further provided herein are ligand-DDB1 complexes. Further provided herein are in vivo modified DDB1 proteins.
Design, synthesis, in vitro and in silico biological assays of new quinazolinone-2-thio-metronidazole derivatives
Ansari, Samira,Asgari, Mohammad Sadegh,Biglar, Mahmood,Esfahani, Ensieh Nasli,Hamedifar, Haleh,Larijani, Bagher,Mahdavi, Mohammad,Mohammadi-Khanaposhtani, Maryam,Rastegar, Hossein,Tas, Recep,Taslimi, Parham
, (2021/07/08)
A new series of quinazolinone-2-thio-metronidazole derivatives 9a-o was designed, synthesized and assayed for their activities against metabolic enzymes human carbonic anhydrase I and II (hCAs I and II), acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and α-glucosidase. The results indicated that all the synthesized compounds exhibited excellent inhibitory activities against mentioned enzymes as compared with standard inhibitors. Representatively, the most potent compound against CA enzymes, 4-fluorophenyl derivative 9i, was 4 and 7-times more potent than standard inhibitor acetazolamide against hCA I and II, respectively; 4-fluorobenzyl derivative 9m as the most potent compound against cholinesterase enzymes, was around 11 and 21-times more potent than standard inhibitor tacrine against AChE and BChE, respectively; the most active α-glucosidase inhibitor 9h with 4-methoxyphenyl moiety was 5-times more active that acarbose as standard inhibitor. Furthermore, in order to study interaction modes of the most potent compounds in the active site of their related enzymes, molecular modeling was performed. Druglikeness, ADME, and toxicity profile of the compounds 9i, 9m, and 9h were also predicted.