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. 2018 Feb 5;57(6):1659-1662.
doi: 10.1002/anie.201710527. Epub 2018 Jan 8.

A General Approach Towards Triazole-Linked Adenosine Diphosphate Ribosylated Peptides and Proteins

Qiang Liu  1 , Hans A V Kistemaker  1   2 , Sagar Bhogaraju  3   4 , Ivan Dikic  3   4 , Herman S Overkleeft  1 , Gijsbert A van der Marel  1 , Huib Ovaa  5 , Gerbrand J van der Heden van Noort  5 , Dmitri V Filippov  1
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A General Approach Towards Triazole-Linked Adenosine Diphosphate Ribosylated Peptides and Proteins

Qiang Liu et al. Angew Chem Int Ed Engl. .

Abstract

Current methods to prepare adenosine diphosphate ribosylated (ADPr) peptides are not generally applicable due to the labile nature of this post-translational modification and its incompatibility with strong acidic conditions used in standard solid-phase peptide synthesis. A general strategy is presented to prepare ADPr peptide analogues based on a copper-catalyzed click reaction between an azide-modified peptide and an alkyne-modified ADPr counterpart. The scope of this approach was expanded to proteins by preparing two ubiquitin ADPr analogues carrying the biological relevant α-glycosidic linkage. Biochemical validation using Legionella effector enzyme SdeA shows that clicked ubiquitin ADPr is well-tolerated and highlights the potential of this strategy to prepare ADPr proteins.

Keywords: ADP-ribosylation; click chemistry; post-translational modification; protein modification; ubiquitination.

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