title: Inhibition of prolyl oligopeptidase with a synthetic unnatural dipeptide.
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.
authors.affiliation: Department of Chemistry, The University of Warwick, Coventry CV47AL, UK.
authors.forename: Daugirdas Tomas
authors.initials: DT
authors.lastname: Racys
authors.forename: Dean
authors.initials: D
authors.lastname: Rea
authors.forename: Vilmos
authors.initials: V
authors.lastname: Fülöp
authors.forename: Martin
authors.initials: M
authors.lastname: Wills
mesh_terms: D001665:Binding Sites; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004151:Dipeptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D011392:Proline / Q000737:chemistry; D000085822:Prolyl Oligopeptidases; D011759:Pyrrolidines / Q000737:chemistry; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000378:metabolism; D015842:Serine Proteinase Inhibitors / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology
chemical_list: D004151:Dipeptides; D011759:Pyrrolidines; D015842:Serine Proteinase Inhibitors; D011392:Proline; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases