Thrombin Inhibitors: Discovery and Design
A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Medicinal Chemistry".
Deadline for manuscript submissions: closed (20 December 2015) | Viewed by 18296
Special Issue Editor
Special Issue Information
Dear Colleagues,
Playing a myriad of procoagulant and anticoagulant roles, thrombin is a central effector in haemostasis and a focal point for blood clotting control, including therapeutic intervention. Given its significant structural similarity to many other serine proteinases carrying out a multitude of disparate tasks, controlling thrombin's behavior with small chemical compounds without interfering with the activity of related enzymes is a formidable challenge. There are, however, many examples of extremely potent and specific thrombin-targeting molecules, namely in the form of natural anticoagulants from haematophagous organisms or from other biological sources. Over the years, many of the unique thrombin recognition and inhibition strategies displayed by these molecules have been unveiled, all while many other synthetic inhibitors have been conceived, developed and perfected. As our knowledge mounts, every new generation of direct thrombin inhibitors brings us closer to the ultimate goal of safely and efficiently modulate thrombin’s activity in a clinical setting. This Special Issue is set to bring together the leading researchers in the fields of discovery and design of specific thrombin inhibitors, helping to disseminate the latest research results and serving as a hub for the establishment of novel and fruitful interactions and collaborations. Original research papers dealing with the discovery, design, characterization, and synthesis of specific thrombin inhibitors are welcome.
Dr. Pedro J. B. Pereira
Guest Editor
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Keywords
- Anticoagulant
- Inhibitor
- thrombin inhibition
- serine proteinase
- structure-guided drug design
- structure-function relationships
- drug discovery
- haemostasis
- blood clotting
- macromolecular recognition
- macromolecular interactions
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