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Enantiomerically Pure Thrombin Inhibitors for Exploring the Molecular-Recognition Features of the Oxyanion Hole

✍ Scribed by Kaspar Schaerer; Martin Morgenthaler; Paul Seiler; Francois Diederich; David W. Banner; Thomas Tschopp; Ulrike Obst-Sander


Publisher
John Wiley and Sons
Year
2005
Weight
14 KB
Volume
36
Category
Article
ISSN
0931-7597

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Structure-activity relationships for new members of a class of nonpeptidic, low-molecular-weight inhibitors of thrombin, a key serine protease in the blood coagulation cascade, are described. These compounds, which originate from X-ray-structure-based design, feature a conformationally rigid, bi-or