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Kistemaker, Hans A. V.; Nardozza, Aurelio Pio; Overkleeft, Herman S.; Marel, Gijs A. van der; Ladurner, Andreas G.; Filippov, Dmitri V. (2016): Synthesis and Macrodomain Binding of Mono-ADP-Ribosylated Peptides. In: Angewandte Chemie-international Edition, Vol. 55, No. 36: pp. 10634-10638
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Mono-ADP-ribosylation is a dynamic posttranslational modification (PTM) with important roles in signaling. Mammalian proteins that recognize or hydrolyze mono-ADP-ribosylated proteins have been described. We report the synthesis of ADP-ribosylated peptides from the proteins histone H2B, RhoA and, HNP-1. An innovative procedure was applied that makes use of pre-phosphorylated amino acid building blocks. Binding assays revealed that the macrodomains of human MacroD2 and TARG1 exhibit distinct specificities for the different ADP-ribosylated peptides, thus showing that the sequence surrounding ADP-ribosylated residues affects the substrate selectivity of macrodomains.