| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1363001 | Bioorganic & Medicinal Chemistry Letters | 2010 | 4 Pages |
Abstract
Most human histamine H3 receptor (hH3R) antagonists follow a general structural blueprint, containing a basic moiety linked by a spacer to a substituted core element. In this investigation the acceptance of thiazol-2-yl ether moieties in the core region is proved with some ether derivatives showing hH3R binding affinities in the nanomolar concentration range. A diversity of structural motifs is used as substituents to enhance the in vitro hH3R binding affinity.
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Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
M. Walter, Y. von Coburg, K. Isensee, K. Sander, X. Ligneau, J.-C. Camelin, J.-C. Schwartz, H. Stark,