ChemBioChem

Cover image for Vol. 16 Issue 2

Editor: Peter Gölitz; Editorial Board Chairs: Thomas Carell, Donald Hilvert, Barbara Imperiali

Online ISSN: 1439-7633

Associated Title(s): ChemCatChem, ChemMedChem, ChemPhysChem, ChemSusChem

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January 15, 2015

Very Important Paper: Synthesis of 3'-Fluoro-tRNA Analogues for Exploring Non-ribosomal Peptide Synthesis in Bacteria

Laura Iannazzo, Guillaume Laisné, Matthieu Fonvielle, Emmanuelle Braud, Jean-Philippe Herbeuval, Michel Arthur, Mélanie Etheve-Quelquejeu*

Among a wide range of metabolic pathways, aminoacyl-tRNAs participate in the synthesis of the peptidoglycan network in the cell wall of bacterial pathogens. To understand the mechanism of these reactions, Mélanie Etheve-Quelquejeu (Université Paris Descartes) and co-workers report on a semi-synthetic route to 3' fluorinated dinucleotides analogues of Ala-tRNAAla with the xylo and ribo configurations and the acylated form of the xylo isomer. The conformation of the 3' fluorinated sugar was also analyzed and it was found that the xylo stereoisomer preferentially adopts a North conformation, while ribo stereoisomers prefer the South conformation.

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Recently Published Articles

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    Karine Nozeret, François Loll, Dr. Christophe Escudé and Prof. Alexandre S. Boutorine

    Article first published online: 30 JAN 2015 | DOI: 10.1002/cbic.201402676

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    Gone FISHing: Hairpin polyamides that target neighboring sites of mouse pericentromeric repeating sequences were synthesized and characterized. Four fluorescently labeled polyamides were selected for pericentromere DNA FISH imaging. Two were successfully used for DNA visualization in living cells.

  2. Establishing the Stability and Reversibility of Protein Pyrophosphorylation with Synthetic Peptides

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    Article first published online: 30 JAN 2015 | DOI: 10.1002/cbic.201402589

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    Back and forth: A series of synthetic pyrophosphopeptides was used to demonstrate the chemical inertness of the pyrophosphoryl group over a large pH range and in the presence of Lewis acidic cations. However, the pyrophosphate group was removed biochemically when the peptides were exposed to alkaline phosphatases, yeast lysates, and mammalian lysates, supporting the idea of reversible protein pyrophosphorylation.

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