83026-93-1Relevant articles and documents
PdII-Catalyzed Purine-Directed Ortho Nitration of 6-Arylpurines by C(sp2)–H Activation: A Practical Approach to Synthesize 6-(2-Nitroaryl)-Purine Derivatives
Gou, Quan,Li, Wenxi,Zhao, Qingsheng,Xie, Jia,Luo, Ping,Cao, Guang,Chen, Suiyun,Qin, Jun
supporting information, p. 4089 - 4094 (2018/08/21)
Herein we report a method for PdII-catalyzed purine-directed ortho nitration of 6-arylpurines via C(sp2)–H activation by using tBuONO/O2 as nitration agent. This procedure is highly efficient and produces a range of 6-(2-nitroaryl)-purine derivatives with good chemoselectivity and functional-group tolerance. The utility of the method is further illustrated in the synthesis of antibacterial agent.
Indole- and Pyrrole-BX: Bench-Stable Hypervalent Iodine Reagents for Heterocycle Umpolung
Caramenti, Paola,Nicolai, Stefano,Waser, Jerome
, p. 14702 - 14706 (2017/09/11)
The one-step synthesis of the bench-stable hypervalent iodine reagents IndoleBX and PyrroleBX using mild Lewis acid catalyzed conditions is reported. The new reagents are stable up to 150 °C and were applied in the C?H arylation of unactivated arenes using either rhodium or ruthenium catalysts. A broad range of heterocyclic systems of high interest for synthetic and medicinal chemistry was accessed in high yields. The developed C?H functionalization could not be achieved using reported reagents or methods, highlighting the unique reactivity of Indole- and Pyrrole-BX.
Synthesis and evaluation of the substrate activity of C-6 substituted purine ribosides with E. coli purine nucleoside phosphorylase: Palladium mediated cross-coupling of organozinc halides with 6-chloropurine nucleosides [1]
Hassan, Abdalla E.A.,Abou-Elkhair, Reham A.I.,Riordan, James M.,Allan, Paula W.,Parker, William B.,Khare, Rashmi,Waud, William R.,Montgomery, John A.,Secrist III, John A.
experimental part, p. 167 - 174 (2012/03/08)
A series of C-6 alkyl, cycloalkyl, and aryl-9-(β-d-ribofuranosyl) purines were synthesized and their substrate activities with Escherichia coli purine nucleoside phosphorylase (E. coli PNP) were evaluated. (Ph 3P)4Pd-mediated cross-c