| Literature DB >> 15509157 |
Elina M Jarho1, Jarkko I Venäläinen, Juhani Huuskonen, Johannes A M Christiaans, J Arturo Garcia-Horsman, Markus M 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.Entities:
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Year: 2004 PMID： 15509157 DOI： 10.1021/jm049503w
Source DB: PubMed Journal: J Med Chem ISSN： 0022-2623 Impact factor: 7.446