Modifying the vicinity of the isopeptide bond to reveal differential behavior of ubiquitin chains with interacting proteins: organic chemistry applied to synthetic proteins

Angew Chem Int Ed Engl. 2013 Oct 11;52(42):11149-53. doi: 10.1002/anie.201306118. Epub 2013 Sep 4.

Abstract

In every direction: Chemical protein synthesis allows the construction of 14 di-ubiquitin analogues modified in the vicinity of the isopeptide bond to examine their behavior with deubiquitinases and ubiquitin binding domains. The results set the ground for the generation of unique probes for studying the interactions of these chains with various ubiquitin-interacting proteins.

Keywords: deubiquitinases; peptide ligation; protein synthesis; ubiquitin chains; ubiquitination.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chemistry, Organic
  • Models, Molecular
  • Peptides / chemical synthesis
  • Peptides / chemistry*
  • Peptides / metabolism
  • Protein Binding
  • Ubiquitin / chemistry*
  • Ubiquitin / metabolism

Substances

  • Peptides
  • Ubiquitin