Possible Thrombus-clearing Mechanism and Modification Suggestion ofβ-sitosterol

The conformational change of EF_loop with the recognition of β-sitosterol effectively occludes the catalytic site, thereby impairing thrombin's proteolytic activity. Among 13 designed sterol derivatives, the compound d3 was identified as a promising inhibitor with excellent ADMET properties. This work provides an anticoagulant mechanism for the dynamic identification of βsitosterol and supports the rational design of allosteric THR inhibitors.