26566-11-0Relevant articles and documents
Total Synthesis of Dansylated Park's Nucleotide for High-Throughput MraY Assays
Wohnig, Stephanie,Spork, Anatol P.,Koppermann, Stefan,Mieskes, Gottfried,Gisch, Nicolas,Jahn, Reinhard,Ducho, Christian
, p. 17813 - 17819 (2016/11/28)
The membrane protein translocase I (MraY) is a key enzyme in bacterial peptidoglycan biosynthesis. It is therefore frequently discussed as a target for the development of novel antibiotics. The screening of compound libraries for the identification of MraY inhibitors is enabled by an established fluorescence-based MraY assay. However, this assay requires a dansylated derivative of the bacterial biosynthetic intermediate Park's nucleotide as the MraY substrate. Isolation of Park's nucleotide from bacteria and subsequent dansylation only furnishes limited amounts of this substrate, thus hampering the high-throughput screening for MraY inhibitors. Accordingly, the efficient provision of dansylated Park's nucleotide is a major bottleneck in the exploration of this promising drug target. In this work, we present the first total synthesis of dansylated Park's nucleotide, affording an unprecedented amount of the target compound for high-throughput MraY assays.
(2S,5R/2R,5S)-Aminoethylpipecolyl aepip-aegPNA chimera: Synthesis and duplex/triplex stability
Shirude, Pravin S.,Kumar, Vaijayanti A.,Ganesh, Krishna N.
, p. 9485 - 9491 (2007/10/03)
This article reports the design and facile synthesis of novel chiral six-membered PNA analogues (2S,5R/2R,5S)-1-(N-Boc-aminoethyl)-5-(thymin-1-yl) pipecolic acid, aepipPNA IV that upon incorporation into standard aegPNA sequences effected stabilization of
