Method for the synthesis of mono-ADP-ribose conjugated peptides

Peter M. Moyle, Tom W. Muir

Research output: Contribution to journalArticlepeer-review

53 Scopus citations


ADP-ribosylation is an important post-translational modification involved in processes including cellular replication, DNA repair, and cell death. Despite these roles, the functions of ADP-ribosylation, in particular mono-ADP-ribosylation, remain poorly understood. The development of a technique to generate large amounts of site-specific, ADP-ribosylated peptides would provide a useful tool for deconvoluting the biochemical roles of ADP-ribosylation. Here we demonstrate that synthetic histone H2B tail peptides, incorporating aminooxy or N-methyl aminooxy functionalized amino acids, can be site-specifically conjugated to ADP-ribose. These peptides are recognized as substrates by the ADP-ribosylation biochemical machinery (PARP1), can interact with the ADP-ribose binding proteins macroH2A1.1 and PARP9, and demonstrate superior enzymatic and chemical stability when compared to ester-linked ADP-ribose. In addition, the incorporation of benzophenone photo-cross-linkers into these peptides is demonstrated to provide a means to probe for and enrich ADP-ribose binding proteins.

Original languageEnglish (US)
Pages (from-to)15878-15880
Number of pages3
JournalJournal of the American Chemical Society
Issue number45
StatePublished - Nov 17 2010
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General Chemistry
  • Biochemistry
  • Catalysis
  • Colloid and Surface Chemistry


Dive into the research topics of 'Method for the synthesis of mono-ADP-ribose conjugated peptides'. Together they form a unique fingerprint.

Cite this