Johanna Rodríguez: The Structural Challenge of Next-Gen Anticoagulants
Johanna Rodríguez, Translational Scientist – Protein Therapeutics and Project Coordination, shared a post on LinkedIn:
“The Structural Challenge of Next-Gen Anticoagulants
For a long time, developing anticoagulants has meant accepting a direct dilemma: if you stop a pathological clot, you inevitably increase the patient’s risk of bleeding.
That is why the structural biology behind Factor XIa is so compelling. Looking at this crystal structure (PDB: 8BO5), you can see the symmetrical homodimer architecture with both catalytic domain pockets highlighted in gold.
Modern drug design targets these specific active site clefts to decouple thrombosis from hemostasis entirely.
By targeting these binding pockets, the goal is to aggressively shut down the contact-activated amplification loop that drives dangerous clots, while leaving the body’s natural, early bleeding control completely intact.
But beautiful 3D models are just the starting point for translational teams. To validate a target and select a clinical dose, you need solid functional data testing on how these dynamics play out in primary human cell assays, platelet activation, and real-time clot composition.”
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