Affiliation:
1. Bio-Organic Synthesis Leiden Institute of Chemistry Leiden University Leiden 2300 RA Netherlands
Abstract
AbstractAdenosine diphosphate (ADP)‐ribosylation is a ubiquitous post‐translational modification that regulates vital biological processes like histone reorganization and DNA‐damage repair through the modification of various amino acid residues. Due to advances in mass‐spectrometry, the collection of long‐known ADP‐ribose (ADPr) acceptor sites, e. g. arginine, cysteine and glutamic acid, has been expanded with serine, tyrosine and histidine, among others. Well‐defined ADPr‐peptides are valuable tools for investigating the exact structures, mechanisms of action and interaction partners of the different flavors of this modification. This review provides a comprehensive overview of synthetic and chemoenzymatic methodologies that enabled the construction of peptides mono‐ADP‐ribosylated on various amino acids, and close mimetics thereof.