Key result
A novel class of sulfonated molecules allosterically inhibited human factor XIa, with inhibitor 16 demonstrating an IC50 of 4.6 µM and good selectivity over other serine proteases.
Why the study?
Factor XIa is targeted to develop new anticoagulants with reduced bleeding risk, but none of the thousands of reported inhibitors have reached the clinic.
Population
Library of 18 sulfonated molecules
Design
In vitro enzyme inhibition and computational study
Authors
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Supports allosteric FXIa targeting for anticoagulation; leaves open in vivo efficacy and clinical translation.
Effect estimate: IC50 4.6 µM
A novel class of sulfonated non-saccharide molecules demonstrates moderate, selective, and allosteric inhibition of human factor XIa in vitro, providing a new platform for anticoagulant drug design.
Al‐Horani et al. (2022) studied Factor XIa inhibition. Sulfonated molecules (inhibitor 16) was evaluated on Inhibition of FXIa (IC50) (IC50 4.6 µM). A novel class of sulfonated molecules allosterically inhibited human factor XIa, with inhibitor 16 demonstrating an IC50 of 4.6 µM and good selectivity over other serine proteases.