Racys, Daurgidas Tomas, Rea, Dean, Fülöp, Vilmos and Wills, Martin (2010) Inhibition of prolyl oligopeptidase with a synthetic unnatural dipeptide. Bioorganic & Medicinal Chemistry, Vol.18 (No.13). pp. 4775-4782. doi:10.1016/j.bmc.2010.05.012 ISSN 0968-0896.

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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.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology
Divisions:	Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) > Biological Sciences ( -2010)
Library of Congress Subject Headings (LCSH):	Enzyme inhibitors -- Research, Biosynthesis -- Research, Enzymes -- Regulation, Piperidine -- Research
Journal or Publication Title:	Bioorganic & Medicinal Chemistry
Publisher:	Elsevier
ISSN:	0968-0896
Official Date:	1 July 2010
Dates:	Date Event 1 July 2010 Published
Volume:	Vol.18
Number:	No.13
Page Range:	pp. 4775-4782
DOI:	10.1016/j.bmc.2010.05.012
Status:	Peer Reviewed
Access rights to Published version:	Restricted or Subscription Access
Funder:	Engineering and Physical Sciences Research Council (EPSRC)

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