A cyclopent-2-enecarbonyl group mimics proline at the P2 position of prolyl oligopeptidase inhibitors.
With the aim to replace the natural amino acid proline by a proline mimetic structure, a cyclopent-2-enecarbonyl moiety was studied at the P2 position of prolyl oligopeptidase (POP) inhibitors. The cyclopent-2-enecarbonyl moiety proved to be an excellent proline mimetic at the P2 position of POP inhibitors. The replacement is particularly useful when increased lipophilicity is needed.
Jarho
Elina M
EM
Department of Pharmaceutical Chemistry, University of Kuopio, P.O. Box 1627, FI-70211 Kuopio, Finland. Elina.Jarho@uku.fi
Venäläinen
Jarkko I
JI
Huuskonen
Juhani
J
Christiaans
Johannes A M
JA
Garcia-Horsman
J Arturo
JA
Forsberg
Markus M
MM
Järvinen
Tomi
T
Gynther
Jukka
J
Männistö
Pekka T
PT
Wallén
Erik A A
EA
D020003:1-Octanol; D000818:Animals; D001921:Brain / Q000187:drug effects / Q000201:enzymology; D002021:Buffers; D003517:Cyclopentanes / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D066298:In Vitro Techniques; D018716:Molecular Mimicry; D011392:Proline / Q000737:chemistry*; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D012995:Solubility; D013329:Structure-Activity Relationship; D013552:Swine
D002021:Buffers; D003517:Cyclopentanes; D015842:Serine Proteinase Inhibitors; D011392:Proline; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases; D020003:1-Octanol