56768-47-9Relevant articles and documents
Cobalt-Catalyzed 1,4-Aryl Migration/Desulfonylation Cascade: Synthesis of α-Aryl Amides
Gillaizeau-Simonian, Nicolas,Barde, Etienne,Guérinot, Amandine,Cossy, Janine
supporting information, p. 4004 - 4008 (2021/02/11)
A cobalt-catalyzed 1,4-aryl migration/disulfonylation cascade applied to α-bromo N-sulfonyl amides was developed. The reaction was highly chemoselective, allowing the preparation of α-aryl amides possessing a variety of functional groups. The method was used as the key step to synthesize an alkaloid, (±)-deoxyeseroline. Mechanistic investigations suggest a radical process.
ADENINE DERIVATIVES AS PROTEIN KINASE INHIBITORS
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Page/Page column 129, (2017/12/14)
The present invention relates to a compound suitable for use as a kinase inhibitor according to general formula (I) [compound (C), herein after], or the N- oxide, pharmaceutically acceptable salt, pharmaceutically acceptable solvate, or stereoisomer thereof, formula (I) wherein A, R1, R2, R3, R3', R4, R4', X, Y, Z, T are as defined in the claims. The invention further relates to an in vitro method of inhibiting protein kinase activity which comprises contacting a protein kinase with a compound of formula (I), or the N-oxide, pharmaceutically acceptable salt, pharmaceutically acceptable solvate, or stereoisomer thereof. The invention further relates to the compounds of formula (I) per se, as well as to their use as a medicament, and for use or in a method of treatment of a disease mediated by a protein kinase selected from cancer, inflammatory disorders, cardiovascular diseases, viral induced diseases, circulatory diseases, fibro-proliferative diseases and pain sensitization disorders.
Active site mapping of trypsin, thrombin and matriptase-2 by sulfamoyl benzamidines
Dosa, Stefan,Stirnberg, Marit,Luelsdorff, Verena,Haeussler, Daniela,Maurer, Eva,Guetschow, Michael
supporting information, p. 6489 - 6505,17 (2012/12/11)
The benzamidine moiety, a well-known arginine mimetic, has been introduced in a variety of ligands, including peptidomimetic inhibitors of trypsin-like serine proteases. According to their primary substrate specificity, the benzamidine residue interacts with the negatively charged aspartate at the bottom of the S1 pocket of such enzymes. Six series of benzamidine derivatives (1-73) were synthesized and evaluated as inhibitors of two prototype serine proteases, that is, bovine trypsin and human thrombin. As a further target, human matriptase-2, a recently discovered type II transmembrane serine protease, was investigated. Matriptase-2 represents an important regulatory protease in iron homeostasis by down-regulation of the hepcidin expression. Compounds 1-73 were designed to contain a fixed sulfamoyl benzamidine moiety as arginine mimetic and a linker-connected additional substructure, such as a tert-butyl ester, carboxylate or second benzamidine functionality. A systematic mapping approach was performed with these inhibitors to scan the active site of the three target proteases. In particular, bisbenzamidines, able to interact with both the S1 and S3/S4 binding sites, showed notable affinity. In branched bisbenzamidines 66-73 containing a third hydrophobic residue, opposite effects of the stereochemistry on trypsin and thrombin inhibition were observed.
