Inhibition of prolyl oligopeptidase with a synthetic unnatural dipeptide
Daugirdas Tomas Racys1, Dean Rea, Vilmos Fülöp
1Department of Chemistry, The University of Warwick, Coventry CV47AL, UK.
Bioorganic & Medicinal Chemistry
|July 15, 2010
Abstract:
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.
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