Marine sulfated glycans (MSGs) are a rich source of novel structures with unique biological activities, particularly in anticoagulation and antithrombosis. MSGs, such as fucosylated chondroitin sulfates (FucCSs) and sulfated fucans (SFs), exhibit anticoagulant properties influenced by their molecular weight, monosaccharide composition, glycosidic linkages, sulfation patterns, and fucosylation levels. Unlike traditional anticoagulants like unfractionated heparin (UFH) and low molecular weight heparin (LMWH), MSGs offer alternative mechanisms, potentially providing a safer therapeutic profile. Despite the recognized anticoagulant potential of MSGs, their binding mechanisms with coagulation factors and the role of metal ions to enhance binding have not been fully explored. This study investigates the binding properties of MSGs from various echinoderm species with key coagulation factors (thrombin, and factor Xa) and serpins (antithrombin, and heparin cofactor II) using surface plasmon resonance. We assessed the inhibitory effects of defined FucCSs and SFs on these interactions, using UFH and LMWH as controls. Our results show that MSGs exhibit antithrombin-independent anticoagulant activity and interact with heparin cofactor II and factor Xa, with metal ions playing a crucial role in some of these bindings. This comprehensive analysis highlights MSGs as promising anticoagulants with potential advantages in safety and efficacy compared to traditional agents.
Ahmed et al. (Tue,) studied this question.