Specific DPP8 and/or DPP9 inhibitors

Dipeptidyl peptidases (DPP's) are essential for many biological processes and are therefore intensively studied within the research community. For this, inhibitors are critically in understanding key functions of this particular family of peptidases. The active site of all members of the DPP-IV family is highly conserved making it difficult to design specific inhibitors.


All available inhibitors the DPP IV family target the catalytic site of these enzymes, acting as competitive inhibitors. As the active site of all members of this family is highly conserved, current inhibitors always show residual activity against other DPPIV homologous. Accordingly, there is still an unmet need for inhibitors that can differentiate between members of the DDPIV family, preferably between DPP8 and DPP9. This is a prerequisite for a selective cancer therapy based on DPP8/9 inhibition.

Our Solution

Scientists at the University of Göttingen developed new and for the first time specific inhibitors of dipeptidyl peptidase 8 and 9, without inhibiting other members of the dipeptidyl peptidase 4 family. The peptide inhibitors show anti-proliverative properties demonstrating their therapeutical usage in cancer therapies.


  • New non-competitive and specific inhibition of DPP8 and DPP9.
  • No background inhibition of DPP IV due to not targeting the catalytic site.
  • No substrate-dependent loss of inhibition effect as with common competitive inhibitors.
  • Cell permeability of active peptide inhibitors - either intrinsic property or achieved with Pep-1 shuttle system.
  • Therapeutic use - Inhibition of cell growth by new peptide inhibitors in tumor cell lines.


  • Use in R&D: Specific inhibition of DPP8 and DPP9 without blocking other members of DPP IV enzyme family.
  • Therapeutical Use: Specific inhibition of DPP8/DPP9 to stop cell growth -> new target for tumor therapy.

Developmental Status

In vitro proof of concept.

Patent Status

A US patent has been granted (Patent holder: University of Göttingen public law foundation).


  • Ross et al.: Structures and mechanism of dipeptidyl peptidases 8 and 9, important players in cellular homeostasis and cancer. PNAS published ahead of print January 30, 2018
  • Pilla et al.: A novel SUMO1-specific interacting motif in Dipeptidyl Peptidase 9 (DPP9) that is important for enzymatic regulation. J Biol Chem. 2012 Dec 28;287(53):44320-9.
  • Pilla et al.: The SUMO1-E67 interacting-loop peptide is an allosteric inhibitor of Dipeptidyl peptidases 8 and 9. J Biol Chem. 2013 Sep 26.
  • US9593148B2


Dr. Stefan Uhle
Patent Manager Life Science
E-Mail: suhle(at)sciencebridge.de
Tel.: +49 551 30724 154
Reference: BioC-1577-UMG

Eine Tochter der