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Inhibition of prolyl oligopeptidase with a synthetic unnatural dipeptide

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

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

Topics: QD, QH301
Publisher: Elsevier
Year: 2010
OAI identifier: oai:wrap.warwick.ac.uk:3307

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