158980-65-5Relevant articles and documents
Divergent response of homologous ATP sites to stereospecific ligand fluorination for selectivity enhancement
Patel, Alpesh Ramanlal,Hardianto, Ari,Ranganathan, Shoba,Liu, Fei
, p. 1570 - 1574 (2017/02/23)
Acquiring a divergent response from homologous protein domains is essential for selective ligand-protein interactions. Stereospecific fluorination of (?)-balanol, an ATP mimic, uncovers a new source of selectivity from integrated chemical and conformational perturbation that differentiates homologous sites by the level of congruency in their response to local and remote fluorine effects.
An efficient formal synthesis of (-)-balanol by using ruthenium-catalyzed asymmetric hydrogenation
Phansavath, Phannarath,De Paule, Sebastien Duprat,Ratovelomanana-Vidal, Virginie,Genet, Jean-Pierre
, p. 3903 - 3907 (2007/10/03)
An efficient formal synthesis of (-)-balanol is reported. The ten-step sequence leading to a key precursor 4 features a highly stereoselective synthesis of the functionalized hexahydroazepine core through dynamic kinetic resolution of a racemic α-amido β-
Total synthesis of (-)-balanol
Miyabe, Hideto,Torieda, Mayumi,Inoue, Kyoko,Tajiri, Kazumi,Kiguchi, Toshiko,Naito, Takeaki
, p. 4397 - 4407 (2007/10/03)
The efficient total synthesis of (-)-balanol, a potent inhibitor of the protein kinase C, is described (-)-Balanol consists of a chiral hexahydroazepine-containing fragment and a benzophenone fragment, both of which were prepared via novel synthetic routes. The hxahydroazepine fragment was prepared in racemic form through either Bu3SnH- or SmI2-promoted radical cyclization of oxime ethers 2ab intramolecularly connected with the formyl group. SmI2-promoted radical cyclization of 2b was found to be particularly successful in the selective synthesis of the seven-membered trans-amino alcohol 8b. Preparation of the enantiomerically pure hexahydroazepine-containing fragment was achieved through the enantioselective enzymatic acetylation of racemic alcohol 9, employing the immobilized lipase from Pseudomonas sp. The benzophenone fragment was prepared in short steps through a biomimetic oxidative anthraquinone ring cleavage starting from commercially available natural chrysophanic acid 15c. This reaction proceeded via [4 + 2]-cycloaddition of single of oxygen to anthracene derivative 17c, followed by Baeyer-Villiger-type rearrangement of the resulting hydroperoxide to afford the benzophenone derivatives 22 and 23.