A Cyclopent-2-enecarbonyl Group Mimics Proline at the P2 Position of Prolyl Oligopeptidase Inhibitors
Journal of Medicinal Chemistry2004Vol. 47(23), pp. 5605–5607
Citations Over TimeTop 19% of 2004 papers
Elina M. Jarho, Jarkko I. Venäläinen, Juhani Huuskonen, Johannes A. M. Christiaans, J. Arturo García‐Horsman, Markus Forsberg, Tomi Järvinen, Jukka Gynther, Pekka T. Männistö, Erik A. A. Wallén
Abstract
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.
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