CHARACTERIZING THE MOLECULAR CHANGES OF THE THROMBIN ACTIVE SITE INDUCED BY THE ALLOSTERIC BINDING OF SULFATED LOW MOLECULAR WEIGHT LIGNINS, A NOVEL CLASS EXOSITE II DIRECT THROMBIN INHIBITORS

Abstract

Recently designed sulfated low molecular weight lignins (LMWLs) function as powerful inhibitors of coagulation through allosteric disruption of thrombin's catalytic activity. Sulfated LMWLs are a unique class of anticoagulants due to their unique molecular scaffold. Prior studies have shown