Structure-based design of amidinophenylurea-derivatives for factor VIIa inhibition
| Autor: | Martin Lorenz, Hans Peter Nestler, Otmar Klingler, Monica Donghi, Manfred Schudok, Herman Schreuder, Hauke Szillat, Joerg Czech, Hans Matter |
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| Rok vydání: | 2004 |
| Předmět: |
Molecular model
Stereochemistry Clinical Biochemistry Pharmaceutical Science Factor VIIa Crystallography X-Ray Biochemistry Chemical synthesis Fibrinolytic Agents Drug Discovery Binding site Molecular Biology Serine protease Binding Sites biology Molecular Structure Chemistry Protease binding Phenylurea Compounds Organic Chemistry Docking (molecular) Enzyme inhibitor Drug Design biology.protein Molecular Medicine Fibrinolytic agent Peptide Hydrolases |
| Zdroj: | Bioorganicmedicinal chemistry letters. 14(14) |
| ISSN: | 0960-894X |
| Popis: | The amidinophenylurea scaffold was earlier shown to provide an excellent template for the synthesis of novel and potent inhibitors of the blood coagulation factor VIIa. In this contribution we describe the structure-based design of potent ligands guided by X-ray crystallography, molecular modeling and docking studies. The design and synthetic efforts were directed towards novel modifications to explore the protease binding region close to the S4 subsite. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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