Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1367368 | Bioorganic & Medicinal Chemistry Letters | 2006 | 5 Pages |
Abstract
A new class of peptidomimetic C5a receptor antagonists characterized by C-terminal amino acids with hydrophobic side chains is presented. Systematic optimization of the first hits led to JPE1375 (36), which was intensively characterized in vitro and in vivo. Compound 36 exhibits high microsomal stability and receptor specificity and is highly active in an immune complex mediated peritonitis model (reverse passive Arthus reaction) in mice.
Graphical abstractNew C5a receptor antagonists characterized by C-terminal amino acids with hydrophobic substitutions are presented.Figure optionsDownload full-size imageDownload as PowerPoint slide
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Karsten Schnatbaum, Elsa Locardi, Dirk Scharn, Uwe Richter, Heiko Hawlisch, Jochen Knolle, Thomas Polakowski,