19914-26-2Relevant articles and documents
Receptor binding mimetics: A novel molecularly imprinted polymer
Kempe, Maria,Mosbach, Klaus
, p. 3563 - 3566 (1995)
A novel molecularly imprinted polymer was prepared by copolymerization of trimethylolpropane trimethacrylate (1) and methacrylic acid (3) in the presence of a dipeptide acting as the template. The recognition capability of the synthetic receptor-like binding sites produced in the polymer network for the peptide was demonstrated by using the polymer as a chiral stationary phase in HPLC. The polymer was superior to previously reported molecularly imprinted polymers in that unusually high racemic resolution and load capacity were demonstrated.
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
supporting information, 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.
