4441-67-2Relevant articles and documents
Ligand-Assisted Palladium(II)/(IV) Oxidation for sp3C H Fluorination
Sun, Huan,Zhang, Yi,Chen, Ping,Wu, Yun-Dong,Zhang, Xinhao,Huang, Yong
, p. 1946 - 1957 (2016/07/06)
The direct functionalization of inert sp3C H bonds is limited to a few bond types. Although the activation of sp3C H bonds can be accomplished under mild conditions using palladium catalysts, the subsequent functionalization is not trivial due to the high energy required to convert palladium(II) to palladium(IV). We have systematically studied the palladium oxidation using computation-guided experiments for reactions involving strong chelation control. We find that a mild external ligand could significantly accelerate the oxidation of palladium(II) to palladium(IV) for strong bidentate directing groups. The acceleration is believed to be a result of ligand stabilization of both the palladium(II) and palladium(IV) intermediates. (Figure presented.) .
Trimethylsilyldiazomethane as a versatile stitching agent for the introduction of aziridines into functionalized organic molecules
Ren, Hong,Wulff, William D.
supporting information; experimental part, p. 4908 - 4911 (2011/02/21)
A highly enantioselective route for the introduction of aziridines into functionalized organic molecules was developed via a tandem acylation and aziridination of TMSCHN2.
α-Aminoalkylphosphonates as a tool in experimental optimisation of P1 side chain shape of potential inhibitors in S1 pocket of leucine- and neutral aminopeptidases
Drag, Marcin,Grembecka, Jolanta,Pawelczak, Malgorzata,Kafarski, Pawel
, p. 764 - 771 (2007/10/03)
The synthesis and biological activity studies of the series of structurally different α-aminoalkylphosphonates were performed in order to optimise the shape of the side chain of the potential inhibitors in S1 pocket of leucine aminopeptidase [E.C.3.4.11.1]. Analysis of a series of compounds with aromatic, aliphatic and alicyclic P1 side chains enabled to find out the structural features, optimal for that fragment of inhibitors of LAP. The most active among all investigated compounds were the phosphonic analogues of homo-tyrosine (Ki = 120:nM) and homo-phenylalanine (Ki = 140:nM), which even as racemic mixtures were better inhibitors in comparison with the best till now-phosphonic analogue of l-leucine (230 nM). Additional comparison of the inhibitory activity obtained for aminopeptidase N (APN, E.C.3.4.11.2) give insight into structural preferences of both enzymes.