Skip to main content
Article thumbnail
Location of Repository

Inhibition of prolyl oligopeptidase with a synthetic unnatural dipeptide

By Daurgidas Tomas Racys, Dean Rea, Vilmos Fülöp and Martin Wills


A new inhibitor, containing a linked proline-piperidine structure, for the enzyme prolyl oligopeptidase (POP) has been synthesised and demonstrated to bind covalently with the enzyme at the active site. This provides evidence that covalent inhibitors of POP do not have to be limited to structures containing five-membered N-containing heterocyclic rings

Topics: QD, QH301
Publisher: Elsevier
Year: 2010
OAI identifier:

Suggested articles


  1. (1996). 36, 746. Supplementary Material Electronic Supplementary Information (ESI) available: [Spectra of new compounds, X-ray details and inhibition testing results]. See DOI:
  2. (2006). Cell Biochemistry and Biophysics doi
  3. (1998). Current Opinion in Structural Biology doi
  4. (1997). Graphics Modell.
  5. (2005). Tetrahedron: Asymmetry
  6. (1994). The CCP4 suite: programs for protein crystallography, doi
  7. The PyMOL User’s Manual 2002, DeLano Scientific,

To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.