Inhibition of prolyl oligopeptidase with a synthetic unnatural dipeptide.
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.
Racys
Daugirdas Tomas
DT
Department of Chemistry, The University of Warwick, Coventry CV47AL, UK.
Rea
Dean
D
Fülöp
Vilmos
V
Wills
Martin
M
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
D004151:Dipeptides; D011759:Pyrrolidines; D015842:Serine Proteinase Inhibitors; D011392:Proline; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases