Issue 36, 2013

Synthesis and biological evaluation of non-isomerizable analogues of Ala-tRNAAla

Abstract

Aminoacyl-tRNAs serve as amino acid donors in many reactions in addition to protein synthesis by the ribosome, including synthesis of the peptidoglycan network in the cell wall of bacterial pathogens. Synthesis of analogs of aminoacylated tRNAs is critical to further improve the mechanism of these reactions. Here we have described the synthesis of two non-isomerizable analogues of Ala-tRNAAla containing an amide bond instead of the isomerizable ester that connects the amino acid with the terminal adenosine in the natural substrate. The non-isomerizable 2′ and 3′ regioisomers were not used as substrates by FemXWv, an alanyl-transferase essential for peptidoglycan synthesis, but inhibited this enzyme with IC50 of 5.8 and 5.5 μM, respectively.

Graphical abstract: Synthesis and biological evaluation of non-isomerizable analogues of Ala-tRNAAla

Article information

Article type
Paper
Submitted
11 Jun 2013
Accepted
22 Jul 2013
First published
08 Aug 2013

Org. Biomol. Chem., 2013,11, 6161-6169

Synthesis and biological evaluation of non-isomerizable analogues of Ala-tRNAAla

D. Mellal, M. Fonvielle, M. Santarem, M. Chemama, Y. Schneider, L. Iannazzo, E. Braud, M. Arthur and M. Etheve-Quelquejeu, Org. Biomol. Chem., 2013, 11, 6161 DOI: 10.1039/C3OB41206G

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