Bioorganic and Medicinal Chemistry Letters p. 2801 - 2805 (2004)
Update date:2022-08-05
Topics:
Nazare, Marc
Matter, Hans
Klingler, Otmar
Al-Obeidi, Fahad
Schreuder, Herman
Zoller, Gerhard
Czech, Joerg
Lorenz, Martin
Dudda, Angela
Peyman, Anusch
Nestler, Hans Peter
Urmann, Matthias
Bauer, Armin
Laux, Volker
Wehner, Volkmar
Will, David W.
A series of novel, highly potent, achiral factor Xa inhibitors based on a benzoic acid scaffold and containing a chlorophenethyl moiety directed towards the protease S1 pocket is described. A number of structural features, such as the requirements of the P1, P4 and ester-binding pocket ligands were explored with respect to inhibition of factor Xa. Compound 46 was found to be the most potent compound in a series of antithrombotic secondary assays.
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