Inhibition of prolyl oligopeptidase with a synthetic unnatural dipeptide.

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Racys DT, Rea D, Fulop V, Wills M

Inhibition of prolyl oligopeptidase with a synthetic unnatural dipeptide.

Bioorg Med Chem. 2010 Jul 1;18(13):4775-82. doi: 10.1016/j.bmc.2010.05.012. Epub 2010 May 31.

PubMed ID

20627594 [ View in PubMed

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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.

DrugBank Data that Cites this Article

Binding Properties

Drug	Target	Property	Measurement	pH	Temperature (°C)
Z-Pro-Prolinal	Prolyl endopeptidase	Ki (nM)	4.3	N/A	N/A	Details