Heparin is a commonly used anticoagulant in treating thromboembolic disease. It binds to various vascular and plasma proteins, such as thrombin and antithrombin, modulating blood coagulation and inflammation. Heparin is typically used in medical patients after an ischemic event and prophylactically for patients at risk for thromboembolism. However, complications may arise such as heparin-induced thrombocytopenia (HIT), which is triggered by both nonimmune and immune responses to heparin. Studying the interactions and binding properties of heparin with vascular and plasma proteins can provide insights that may be useful for reducing the risk of heparin-induced adverse events. In this study, fluorescence spectroscopy was used to quantify and characterize the heparin-binding capacity of the major plasma protein, fibrinogen, and of the platelet receptor, TLT-1. Electrophoretic mobility shift assays (EMSAs) were employed to visualize the in-solution, heparin-protein interactions. This study also describes methods for synthesizing two coumarin derived, α-dicarbonyl compounds as pH and polarity sensors to label arginine residues on proteins of interest for concurrent heparin-binding studies.

Method development for studying the interactions and binding properties of heparin with plasma and platelet proteins

ACS Spring Meeting 2021

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