Rapid optimization of labeled ubiquitinated peptides for monitoring deubiquitinases activities

Org Biomol Chem. 2015 Aug 14;13(30):8182-6. doi: 10.1039/c5ob01142f.

Abstract

Studying and targeting deubiquitinases is of high importance due to their various roles in cellular processes and involvement in diseases such as cancer. The recent development of unique probes and reagents using chemical synthesis of proteins became very instrumental in supporting these efforts. Here, we present a protein synthetic approach that enables the rapid synthesis of differently modified labeled-ubiquitinated peptides to facilitate rapid optimization of deubiquitinase substrates.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Chromatography, High Pressure Liquid
  • Kinetics
  • Molecular Sequence Data
  • Peptide Library
  • Peptides / chemical synthesis*
  • Peptides / chemistry
  • Spectrometry, Mass, Electrospray Ionization
  • Staining and Labeling*
  • Substrate Specificity
  • Ubiquitin-Specific Proteases / metabolism*
  • Ubiquitination*

Substances

  • Peptide Library
  • Peptides
  • Ubiquitin-Specific Proteases