Profiling of protein synthesis and degradation - cell-wide!
  • The human proteome is a highly interactive and dynamic system. Individual protein amounts reflect the complex homeostasis of synthesis and degradation
  • Approximately 50 percent of the proteome is thought to play a role in human disease and yet was so far inaccessible to treatment
  • Just now, therapeutics are developed to modulate target protein stability, a new tool to "drug the undruggable", including PROTACs ("proteolysis targeting chimera"), and other small molecules
  • TurnoverScout™ enables tracking of protein synthesis and degradation independently, at the same time, for more than 8,000 cellular proteins in parallel
  • TurnoverScout™ is based on pulse-chase labelling of newly synthesized proteins with heavy amino acids
  • TurnoverScout™ can be combined with enrichment technologies for proteins (e.g. by immobilized ligand binding), or their post-translational modification (e.g. by phospho-proteomics) for higher sensitivity
  • TurnoverScout™ allows deep insights into treatment-induced effects on cellular protein homeostasis


Further reading

Oprea et al (2018). Unexplored therapeutic opportunities in the human genome, Nature Reviews Drug Discovery, 17(5):317-332. [Link]

Zecha, J., Meng C., Zolg D.P., Samaras P., Wilhelm M., Kuster B. (2017). Peptide level turnover measurements enable the study of proteoform dynamics. 17(5):974-992. [Link]

Savitski, M.M. et al. (2018). Multiplexed proteome dynamics profiling reveals mechanisms controlling protein homeostasis. Cell 173(1):260-274.e25 [Link]

Protein degradation kinetics of two regulatory proteins
With our TurnoverScout technology, we enable the proteome-wide analysis of protein synthesis and degradation upon cellular perturbation. You can identify the target(s) of such MoAs and optimize leads that result in the selective degradation of the desired target.